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ADP + H2O + a folded polypeptide
AMP + phosphate + an unfolded polypeptide
ADP + phosphate + unfolded actin
ATP + H2O + folded actin
ADP + phosphate + unfolded tubulin
ATP + H2O + folded tubulin
AMP + H2O
adenosine + phosphate
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
ATP + H2O + folded 5(6)-carboxytetramethylrhodamine-tagged bacteriorhodopsin peptide
ADP + phosphate + unfolded 5(6)-carboxytetramethylrhodamine-tagged bacteriorhodopsin peptide
-
i.e. 5(6)-carboxytetramethylrhodamine-KKAITTLVPAIAFTMYLSMLLKK
-
-
?
ATP + H2O + folded aldohexose dehydrogenase
ADP + phosphate + unfolded aldohexose dehydrogenase
-
-
-
?
ATP + H2O + folded CF1gamma polypeptide
ADP + phosphate + unfolded CF1gamma polypeptide
-
-
-
-
?
ATP + H2O + folded indole-3-glycerol-phosphate synthase
ADP + phosphate + unfolded indole-3-glycerol-phosphate synthase
ATP + H2O + folded malate dehydrogenase
ADP + phosphate + unfolded malate dehydrogenase
ATP + H2O + folded phosphate-binding protein
ADP + phosphate + unfolded phosphate-binding protein
-
-
-
-
?
ATP + H2O + folded rhamnose dehydrogenase
ADP + phosphate + unfolded rhamnose dehydrogenase
-
-
-
?
CTP + H2O + a folded polypeptid
CDP + phosphate + an unfolded polypeptide
-
-
-
?
CTP + H2O + a folded polypeptide
CDP + phosphate + an unfolded polypeptide
GTP + H2O + a folded polypeptide
GDP + phosphate + an unfolded polypeptide
IDP + H2O + a folded polypeptide
IMP + phosphate + an unfolded polypeptide
-
-
-
?
ITP + H2O + a folded polypeptide
IDP + phosphate + an unfolded polypeptide
-
-
-
?
UTP + H2O + a folded polypeptide
UDP + phosphate + an unfolded polypeptide
additional information
?
-
ADP + H2O + a folded polypeptide
AMP + phosphate + an unfolded polypeptide
-
-
-
-
ir
ADP + H2O + a folded polypeptide
AMP + phosphate + an unfolded polypeptide
-
-
-
-
ir
ADP + H2O + a folded polypeptide
AMP + phosphate + an unfolded polypeptide
-
-
-
-
ir
ADP + H2O + a folded polypeptide
AMP + phosphate + an unfolded polypeptide
-
-
-
-
ir
ADP + H2O + a folded polypeptide
AMP + phosphate + an unfolded polypeptide
ADPase activity in presence of Co2+, almost no hydrolysis in presence of Mn2+ or Mg2+, monomeric enzyme form
-
-
?
ADP + H2O + a folded polypeptide
AMP + phosphate + an unfolded polypeptide
ADPase activity in presence of Co2+, Mn2+ or Mg2+, monomeric enzyme form
-
-
?
ADP + phosphate + unfolded actin
ATP + H2O + folded actin
-
-
-
-
?
ADP + phosphate + unfolded actin
ATP + H2O + folded actin
-
-
-
-
?
ADP + phosphate + unfolded actin
ATP + H2O + folded actin
-
-
-
-
?
ADP + phosphate + unfolded actin
ATP + H2O + folded actin
-
-
-
-
?
ADP + phosphate + unfolded tubulin
ATP + H2O + folded tubulin
-
-
-
-
?
ADP + phosphate + unfolded tubulin
ATP + H2O + folded tubulin
-
-
-
-
?
ADP + phosphate + unfolded tubulin
ATP + H2O + folded tubulin
-
-
-
-
?
ADP + phosphate + unfolded tubulin
ATP + H2O + folded tubulin
-
-
-
-
?
AMP + H2O
adenosine + phosphate
AMPase activity in presence of Co2+, almost no hydrolysis in presence of Mn2+ or Mg2+, monomeric enzyme form
-
-
?
AMP + H2O
adenosine + phosphate
AMPase activity in presence of Co2+, Mn2+ or Mg2+, monomeric enzyme form
-
-
?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
-
-
?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
-
-
-
?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
-
-
?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
-
-
-
?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
-
-
-
?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
-
-
?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
-
-
-
?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
GroEL participates in bacterial temperature adaption
-
-
?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
-
-
?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
-
-
?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
-
-
-
?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
-
-
-
?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
-
-
?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
-
-
?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
-
-
?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
-
-
-
?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
-
-
?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
-
-
-
ir
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
-
-
?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
-
-
?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
-
-
?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
-
-
?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
-
-
?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
-
-
?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
-
-
?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
-
-
?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
-
-
?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
-
-
?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
-
-
?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
-
-
?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
-
-
?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
-
654461, 654810, 654945, 669221, 699525, 719957, 733278, 733538, 733876, 734278, 735006, 735322, 750069, 751195, 751329, 752285 -
-
?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
-
-
-
ir
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
-
-
?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
-
-
?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
aconitase B, bind transiently to GroEL and probably doesn´t require ATP and GroES
-
-
?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
bovine rhodanese
-
-
?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
MetE, bind transiently to GroEL and probably doesn´t require ATP and GroES
-
-
?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
pig heart malate dehydrogenase
-
-
?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
aconitase, requires GroEL, co-chaperonin GroES and ATP for complete folding
-
-
?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
assay at 24°C
-
-
?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
assay at pH 7.4, 23°C, 5 min
-
-
?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
beta-galactosidase, bind transiently to GroEL and probably doesn´t require ATP and GroES
-
-
?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
decarboxylase component E1, requires GroEL, co-chaperonin GroES and ATP for complete folding
-
-
?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
dependent on protein if ATP release substrate from GroEL or if complete chaperonin system GroEL-GroES and ATP is required
-
-
?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
green fluorescent protein, requires GroEL, co-chaperonin GroES and ATP for complete folding
-
-
?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
high affinity in taut state
-
-
?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
malate dehydrogenase
-
-
?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
maltodextrin glucosidase, requires GroEL, co-chaperonin GroES and ATP for complete folding
-
-
?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
P22 tail spike protein, interacts with GroEL and gets released by action of nucleotide alone
-
-
?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
phytochrome photoreceptor, interacts with GroEL and gets released by action of nucleotide alone
-
-
?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
rhodanese
-
-
?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
RUBISCO, requires GroEL, co-chaperonin GroES and ATP for complete folding
-
-
?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
strong binding peptide
-
-
?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
strong binding peptide W2DP6V
-
-
?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
folding of the model substrate HippelLindau tumor suppressor protein VHL in an ATP-dependent manner. Heterogeneity of the action of GroES/EL on a bound polypeptide substrate might arise from the random nature of the specific binding to the various identical subunits of GroEL, and might help explain why multiple rounds of binding and hydrolysis are required for some chaperonin substrates
-
-
?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
the equilibrium and kinetics of MgATP2- binding to GroEL mutant Y485W is studied via isothermal titration calorimetry (ITC) and stopped-flow fluorescence spectroscopy. Comparison of the kinetics in the absence and presence of K+ clearly demonstrate that the first fluorescence-increasing phase corresponds to bimolecular MgATP2- binding to GroEL
-
-
?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
the GroEL/GroES protein folding chamber is formed and dissociated by ATP binding and hydrolysis. ATP hydrolysis in the GroES-bound (cis) ring gates entry of ATP into the opposite unoccupied trans ring, which allosterically ejects cis ligands. ADP release from the cis ring is not the rate-limiting step of the GroEL/GroES reaction cycle
-
-
?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
ATP is an allosteric ligand for GroEL, its binding promoting both cooperative (intra-ring) and anti-cooperative (inter-ring) actions. ATP serves as a substrate, undergoing hydrolysis during the reaction cycle to promote a unidirectional advance of the machine. Inter-ring contacts in the ATPase cycle, modeling, overview
-
-
?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
GroEL is an ATP-driven macromolecular machine. GroEL and its bound cofactor GroES undergo an ATP-regulated interaction cycle that serves to close and open the folding cage. In the asymmetric reaction mode, only one ring of GroEL is GroES bound and the two rings function sequentially, coupled by negative allostery. In the symmetric mode, both GroEL rings are GroES bound and are folding active simultaneously. GroEL:GroES stoichiometry calculation: symmetric GroEL:GroES2 complexes are substantially populated only in the presence of non-foldable model proteins, such as alpha-lactalbumin and alpha-casein, which overstimulate the GroEL ATPase and uncouple the negative GroEL inter-ring allostery. In contrast, asymmetric complexes are dominant both in the absence of substrate and in the presence of foldable substrate proteins. Upon binding of ATP to GroEL, GroES caps the GroEL ring that holds the substrate (cis-ring), resulting in its displacement into an enclosed chamber large enough for proteins up to 60 kDa
-
-
?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
GroEL, non-native protein, and GroES undergo ATP-regulated binding and release cycles
-
-
?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
chimeric fluorescent protein CYPet-YPet, assay at pH 7.5, 25°C
-
-
?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
high affinity in taut state
-
-
?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
-
-
?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
-
-
?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
-
-
-
ir
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
-
-
-
ir
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
-
-
-
?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
-
-
?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
ATP hydrolysis is not essentially required for protein folding, i.e. chaperone activity of Mm-cpn
-
-
?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
Mm-cpn also hydrolyzes with slightly weaker activity CTP, UTP and GTP
-
-
?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
structures of a group II chaperonin in both open (nucleotide-free) and closed (ATP-induced) states at unprecedented resolutions by single particle cryo-EM and computational modeling reveals that in group II chaperonins the key structural rearrangements leading from the open to closed state are completely different from those found in group I chaperonins, despite structural similarities between the groups
-
-
?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
ATP hydrolysis has a dual role in group II chaperonin function, promoting both lid closure and release of the substrate into the cavity. Importantly, both events must occur for successful substrate folding. An alternate model for group II chaperonin function is suggested, whereby folding relies on the release of the substrate into a unique chemical environment within the closed chamber
-
-
?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
the structure of an archaeal group II chaperonin in its prehydrolysis ATP-bound state at subnanometer resolution using single particle cryo-electron microscopyis reported. Structural comparison of Mm-cpn in ATP-free, ATP-bound, and ATP-hydrolysis states reveals that ATP binding alone causes the chaperonin to close slightly with a 45° counterclockwise rotation of the apical domain. The subsequent ATP hydrolysis drives each subunit to rock toward the folding chamber and to close the lid completely
-
-
?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
the archaeal GroEL/GroES system has preserved the basic encapsulation mechanism of bacterial GroEL and suggest that it has adjusted the length of its reaction cycle to the slower growth rates of Archaea. The release of only folded protein from the GroEL/GroES cage would avoid non-productive interactions of the GroEL substrates with the thermosome, which is not normally located within the same compartment
-
-
?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
optimal functionality of MmGroEL/GroES and its ability to encapsulate larger proteins, such as malate dehydrogenase, requires the presence of ammonium sulfate in vitro
-
-
?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
-
-
?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
-
-
-
?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
-
-
?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
-
-
?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
-
-
-
?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
-
-
?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
-
-
?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
-
-
?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
-
-
?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
-
-
-
?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
-
-
-
?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
-
-
?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
-
-
-
ir
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
-
-
ir
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
Pf Cpn protects protein from inactivation and aggregation in an ATP dependent manner
-
-
?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
chaperonin activity in protecting lysozyme from heat-induced inactivation
-
-
?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
Pf Cpn binds specifically to denatured lysozyme. ATP addition results in protection of lysozyme from aggregation and inactivation at 100°C. While complexed to heat inactivated lysozyme, Pf Cpn shows enhanced ATPase activity
-
-
?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
-
-
-
ir
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
-
-
-
?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
-
-
-
?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
a phosphorylated intermediate of enzyme exists during hydrolysis
-
-
?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
-
-
?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
-
-
?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
-
-
-
?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
the enzyme assists the folding of actins, tubulins, and other proteins in an ATP-dependent manner
-
-
?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
ATPase-dependent folding of the cytoskeletal protein actin
-
-
?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
-
-
?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
-
-
?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
-
-
?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
-
-
?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
Tequatrovirus T4
-
assay at 24°C
-
-
?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
-
-
?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
-
-
?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
-
-
-
?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
-
-
-
ir
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
folding of green fluorescent protein, assay at 60°C, 10 min
-
-
?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
the chaperonin heterooligomer Cpnab (containing both alpha and beta in the alternate order) protects citrate synthase from thermal aggregation, promotes the folding of acid-denatured Green fluorescence protein in an ATP-dependent manner, and exhibits an ATP-dependent conformational change
-
-
?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
the chaperonin heterooligomer Cpnab (containing both alpha and beta in the alternate order) protects citrate synthase from thermal aggregation, promotes the folding of acid-denatured Green fluorescence protein in an ATP-dependent manner, and exhibits an ATP-dependent conformational change
-
-
?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
-
-
-
?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
folding of green fluorescent protein, assay at 60°C, 10 min
-
-
?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
the chaperonin heterooligomer Cpnab (containing both alpha and beta in the alternate order) protects citrate synthase from thermal aggregation, promotes the folding of acid-denatured Green fluorescence protein in an ATP-dependent manner, and exhibits an ATP-dependent conformational change
-
-
?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
-
-
?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
-
-
-
ir
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
-
-
?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
-
-
?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
60°C, assay at pH 7.0, 90 min, 0,12 mM released phosphate
-
-
?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
folding of green fluorescent protein, 50°C, assay at pH 7.0
-
-
?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
folding of malate dehydrogenase, 50°C, assay at pH 7.0
-
-
?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
-
-
?
ATP + H2O + folded indole-3-glycerol-phosphate synthase
ADP + phosphate + unfolded indole-3-glycerol-phosphate synthase
-
-
-
-
?
ATP + H2O + folded indole-3-glycerol-phosphate synthase
ADP + phosphate + unfolded indole-3-glycerol-phosphate synthase
-
-
-
-
?
ATP + H2O + folded malate dehydrogenase
ADP + phosphate + unfolded malate dehydrogenase
-
-
-
-
?
ATP + H2O + folded malate dehydrogenase
ADP + phosphate + unfolded malate dehydrogenase
-
-
-
-
?
ATP + H2O + folded malate dehydrogenase
ADP + phosphate + unfolded malate dehydrogenase
-
-
-
-
?
CTP + H2O + a folded polypeptide
CDP + phosphate + an unfolded polypeptide
-
-
-
?
CTP + H2O + a folded polypeptide
CDP + phosphate + an unfolded polypeptide
-
5 mM Mg2+, 90 min, 0.1 mM released phosphate
-
-
?
GTP + H2O + a folded polypeptide
GDP + phosphate + an unfolded polypeptide
-
-
-
?
GTP + H2O + a folded polypeptide
GDP + phosphate + an unfolded polypeptide
-
5 mM Mg2+, 0.07 mM released phosphate after 90 min
-
-
?
UTP + H2O + a folded polypeptide
UDP + phosphate + an unfolded polypeptide
-
-
-
?
UTP + H2O + a folded polypeptide
UDP + phosphate + an unfolded polypeptide
-
5 mM Mg2+, 90 min, 0.11 mM released phosphate
-
-
?
additional information
?
-
-
the recombinant ApcpnA protects thermal inactivation of yeast alcohol dehydrogenase and bovine liver rhodanese as substrate proteins
-
-
?
additional information
?
-
-
enzyme catalyzes refolding of denatured malate dehydrogenase into the active form
-
-
?
additional information
?
-
-
factors governing the substrate recognition by GroEL chaperone. The presence of single or multiple GroES mobile looplike hydrophobic patches in the amino acid sequence seems to be a foremost criterion for a protein to be recognized by GroEL. The hydrophobic region on the protein must also be exposed in its nonnative form so that it can interact with the peptide-binding region on the GroELs apical domain
-
-
?
additional information
?
-
-
GroEL binds only one molecule of the model substrate Rubisco. In contrast, the capsid protein of bacteriophage T4, a natural GroEL substrate, can occupy both rings simultaneously. Each substrate induces distinct conformational changes in the GroEL chaperonin. Binding of Rubisco to the GroEL oligomer stabilizes the chaperonin complex significantly, whereas binding of one capsid protein does not have the same effect. Addition of a second capsid protein molecule to GroEL results in a similar stabilizing effect to that obtained after the binding of a single Rubisco. The binding of a single capsid polypeptide does not induce significant conformational changes in the GroEL trans ring, and hence the unoccupied GroEL ring remains accessible for a second capsid molecule
-
-
?
additional information
?
-
-
GroEL interacts strongly with the enzyme rhodanese undergoing thermal unfolding at 43°C. The enzyme forms a binary complex. Active rhodanese (82%) could be recovered by releasing the enzyme from GroEL after the addition of several components, e.g. ATP and the co-chaperonin GroES. The inability to recover active enzyme at 43°C from the GroELrhodanese complex is not due to the disruption of the complex or aggregation of rhodanese, but rather to the partial loss of its ATPase activity and/or to the inability of rhodanese to be released from GroEL due to a conformational change
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?
additional information
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GroES-assisted refolding of unfolded zinc-cytochrome c takes place by a mechanism that is quite close to the Anfinsen Cage hypothesis for molecular chaperone activity. Even in the presence of ATP, GroEL/GroES-assisted refolding of ZnCyt c takes place at approximately half the rate of refolding of ZnCyt c alone. All forward rate enhancements or reductions could be accounted for in terms of thermodynamic coupling due to binding interactions between GroEL and unfolded protein substrates,driven by thermodynamic considerations. It is proposed that passive kinetic partitioning should be considered the core mechanism of the GroEL/GroES molecular chaperone machinery, wherein the core function is to bind unfolded protein substrates leading to a blockade of aggregation pathways and to increases in molecular flux through productive folding pathways
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?
additional information
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the bound state of isotope-labeled human dihydrofolate reductase includes random coil conformations devoid of stable native-likle tertiary contacts and may be best described as a dynamic ensemble of randomly structured conformers
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?
additional information
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GroEL-GroES interaction is analyzed: using a unique strategy to create GroES variants with various affinities for GroEL a direct role of GroES in facilitating substrate folding through its dynamics with GroEL is indicated
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?
additional information
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malate dehydrogenase and rhodanase are substrate proteins for GroEl refolding
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?
additional information
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the GroEL/ES system promotes protein folding, mechanism overview
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?
additional information
?
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the apical GroEL domain (residues 191-376) binds cofactor non-native substrate protein, helices H (residues 233-243) and I (residues 255-267) of the apical domains expose multiple hydrophobic amino acids towards the ring center, forming a circular surface for the binding of a non- native substrate protein, GroEL/ES cycling in the presence of substrate, overview. The C-terminal Gly-Gly-Met repeat sequences are also required for accelerated folding
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?
additional information
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the presence of non-native substrate protein alters the GroEL/ES reaction by shifting it from asymmetric to symmetric complexes. Substrate proteins are mutant maltose binding protein, Rhodospirillium rubrum ribulose-1,5-bisphosphat-carboxylase/-oxygenase, mitochondrial malate dehydrogenase, mitochondrial rhodanese, alpha-lactalbumin, and alpha-casein
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?
additional information
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the refolding of urea-denatured rhodanese is catalyzed by the wild-type enzyme, and also at low temperatures by oxidized GroEL, which contains increased exposed hydrophobic surfaces and retains its ability to hydrolyse ATP. Oxidized GroEL efficiently binds the urea-unfolded rhodanese at 4°C, without requiring excess amount of chaperonin relative to normal GroEL (i.e. non-oxidized). The loss of the ATPase activity of oxidized GroEL at 4°C prevents the release of rhodanese from the GroEL-rhodanese complex
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?
additional information
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the recombinant enzyme possesses ATPase activity and contributes to the refolding of recombinant MG PrpC protein
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additional information
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the recombinant enzyme possesses ATPase activity and contributes to the refolding of recombinant MG PrpC protein
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additional information
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the recombinant enzyme possesses ATPase activity and contributes to the refolding of recombinant MG PrpC protein
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additional information
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PfCPN has almost no ADPase activity
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additional information
?
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enzyme has two distinct conformational states that are part of chaperonin functional cycle. The closed archaeosome complex binds ATP and forms an open complex. Upon ATP hydrolysis, the open complex dissociates into subunits. Free subunits reassemble into a two-ring structure. Denatured proteins associate with both conformational states as well as with free subunits that form an intermediate complex
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additional information
?
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enzyme is an RNA-binding protein that interacts specifically in vivo with the 16S rRNA and participates in the maturation of its 5' extremity in vitro. The chaperonin binds RNA as the native heterooligomeric complex and RNA binding and processing are inhibited by ATP
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?
additional information
?
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study on aggregation and inactivation of monomeric model proteins chicken egg white lysozyme and yeast alpha-glucosidase, and tetrameric model proteins chicken liver malic enzyme, and yeast alcohol dehydrogenase. The chaperonin has nonequivalent surfaces for the binding of the model proteins upon heating: the thermal denaturation intermediates of the single-chain proteins share surfaces I, while the thermal denaturation intermediates of the tetrameric proteins share surfaces II. ATP binding to the chaperonin induces a conformation that lacks surfaces I and carries surfaces II. Enzyme shows two mechanistically distinct strategies, one being ATP-dependent and the other ATP-independent
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additional information
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chaperonin completely inhibits spontaneous refoldings of several denatured proteins and suppresses aggregation upon dilution of the denaturant, refoldings resume upon ATP hydrolysis, with yields of active molecules and rates of folding notably higher than in spontaneous processes. Chaperonin prevents the irreversible inactivations at 90°C of several thermophilic enzymes by the binding of the denaturation intermediate, the timecourses of inactivations are unaffected and most activity is regained upon hydrolysis of ATP. Chaperonin completely prevents the formation of aggregates during thermal inactivation of chicken egg white lysozyme at 70°C, without affecting the rate of activity loss. ATP hydrolysis results in the recovery of most lytic activity
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additional information
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a novel spectroscopic assay through selectively labeling the C terminus of yeast actin with acrylodan and observe significant changes in the acrylodan fluorescence emission spectrum as actin is chemically unfolded and then refolded by the chaperonin. Variation in the polarity of the environment surrounding the fluorescent probe during the unfolding/folding processes allows to monitor actin as it folds on CCT
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additional information
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enzyme inhibits the spontaneous refolding of lactate dehydrogenase denatured with 6.4 M guanidine HCl. The addition of ATP does not enhance the degree of refolding
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additional information
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enzyme inhibits the spontaneous refolding of lactate dehydrogenase denatured with 6.4 M guanidine HCl. The addition of ATP does not enhance the degree of refolding
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?
additional information
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enzyme inhibits the spontaneous refolding of lactate dehydrogenase denatured with 6.4 M guanidine HCl. The addition of ATP does not enhance the degree of refolding
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?
additional information
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enzyme inhibits the spontaneous refolding of lactate dehydrogenase denatured with 6.4 M guanidine HCl. The addition of ATP does not enhance the degree of refolding
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additional information
?
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additional ATP-dependent protein refolding activity and suppression of rhodanese and luciferase thermal aggregation
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additional information
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the chaperonins GroEL and GroES are essential mediators of protein folding. GroEL binds nonnative protein, ATP, and GroES, generating a ternary complex in which protein folding occurs within the cavity capped by GroES
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Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
ADP + H2O + a folded polypeptide
AMP + phosphate + an unfolded polypeptide
ADP + phosphate + unfolded actin
ATP + H2O + folded actin
ADP + phosphate + unfolded tubulin
ATP + H2O + folded tubulin
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
additional information
?
-
ADP + H2O + a folded polypeptide
AMP + phosphate + an unfolded polypeptide
-
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ir
ADP + H2O + a folded polypeptide
AMP + phosphate + an unfolded polypeptide
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-
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ir
ADP + H2O + a folded polypeptide
AMP + phosphate + an unfolded polypeptide
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-
-
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ir
ADP + H2O + a folded polypeptide
AMP + phosphate + an unfolded polypeptide
-
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ir
ADP + phosphate + unfolded actin
ATP + H2O + folded actin
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-
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?
ADP + phosphate + unfolded actin
ATP + H2O + folded actin
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-
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?
ADP + phosphate + unfolded actin
ATP + H2O + folded actin
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-
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?
ADP + phosphate + unfolded actin
ATP + H2O + folded actin
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-
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-
?
ADP + phosphate + unfolded tubulin
ATP + H2O + folded tubulin
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-
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?
ADP + phosphate + unfolded tubulin
ATP + H2O + folded tubulin
-
-
-
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?
ADP + phosphate + unfolded tubulin
ATP + H2O + folded tubulin
-
-
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-
?
ADP + phosphate + unfolded tubulin
ATP + H2O + folded tubulin
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?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
-
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?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
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-
?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
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-
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?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
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-
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?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
-
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?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
GroEL participates in bacterial temperature adaption
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?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
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?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
-
-
?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
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-
-
-
?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
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-
-
-
?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
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-
-
?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
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-
-
?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
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-
-
?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
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-
-
-
?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
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-
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?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
-
-
-
ir
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
-
-
?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
-
-
?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
-
-
?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
-
-
?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
-
-
?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
-
-
?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
-
-
?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
-
-
?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
-
-
?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
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-
?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
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-
-
?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
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-
?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
-
-
?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
-
654461, 654810, 654945, 733278, 733538, 733876, 734278, 735006, 735322, 750069, 751195, 751329, 752285 -
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?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
-
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ir
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
-
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?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
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-
-
?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
aconitase B, bind transiently to GroEL and probably doesn´t require ATP and GroES
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?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
bovine rhodanese
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?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
MetE, bind transiently to GroEL and probably doesn´t require ATP and GroES
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?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
pig heart malate dehydrogenase
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?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
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?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
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-
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?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
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ir
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
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ir
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
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?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
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?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
the archaeal GroEL/GroES system has preserved the basic encapsulation mechanism of bacterial GroEL and suggest that it has adjusted the length of its reaction cycle to the slower growth rates of Archaea. The release of only folded protein from the GroEL/GroES cage would avoid non-productive interactions of the GroEL substrates with the thermosome, which is not normally located within the same compartment
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?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
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?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
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-
-
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?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
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?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
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?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
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?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
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?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
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-
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?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
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-
-
?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
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-
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?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
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-
-
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?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
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-
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?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
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-
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ir
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
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ir
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
Pf Cpn protects protein from inactivation and aggregation in an ATP dependent manner
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ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
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ir
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
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-
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?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
-
-
?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
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-
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?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
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?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
the enzyme assists the folding of actins, tubulins, and other proteins in an ATP-dependent manner
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?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
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?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
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?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
-
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?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
-
-
?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
-
-
-
?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
-
-
-
ir
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
-
-
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?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
-
-
?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
-
-
-
ir
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
-
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?
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
-
-
-
?
additional information
?
-
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GroEL-GroES interaction is analyzed: using a unique strategy to create GroES variants with various affinities for GroEL a direct role of GroES in facilitating substrate folding through its dynamics with GroEL is indicated
-
-
?
additional information
?
-
-
malate dehydrogenase and rhodanase are substrate proteins for GroEl refolding
-
-
?
additional information
?
-
-
the GroEL/ES system promotes protein folding, mechanism overview
-
-
?
additional information
?
-
-
enzyme has two distinct conformational states that are part of chaperonin functional cycle. The closed archaeosome complex binds ATP and forms an open complex. Upon ATP hydrolysis, the open complex dissociates into subunits. Free subunits reassemble into a two-ring structure. Denatured proteins associate with both conformational states as well as with free subunits that form an intermediate complex
-
-
?
additional information
?
-
-
enzyme is an RNA-binding protein that interacts specifically in vivo with the 16S rRNA and participates in the maturation of its 5' extremity in vitro. The chaperonin binds RNA as the native heterooligomeric complex and RNA binding and processing are inhibited by ATP
-
-
?
additional information
?
-
-
study on aggregation and inactivation of monomeric model proteins chicken egg white lysozyme and yeast alpha-glucosidase, and tetrameric model proteins chicken liver malic enzyme, and yeast alcohol dehydrogenase. The chaperonin has nonequivalent surfaces for the binding of the model proteins upon heating: the thermal denaturation intermediates of the single-chain proteins share surfaces I, while the thermal denaturation intermediates of the tetrameric proteins share surfaces II. ATP binding to the chaperonin induces a conformation that lacks surfaces I and carries surfaces II. Enzyme shows two mechanistically distinct strategies, one being ATP-dependent and the other ATP-independent
-
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?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
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R285H
-
no significant difference in the refolding activity between mutant and wild-type GroEL
T93I
-
no significant difference in the refolding activity between mutant and wild-type GroEL. No significant difference in inorganic phosphate release between mutant and wild-type enzyme at 10°C, 37°C and 50°C
D373A
-
the thermostability of the mutant is compromised as it retains 4.7% of the basal ATPase activity of the wild type enzyme after 1 h incubation at 65°C
L439A
-
the thermostability of the mutant is compromised as it retains about 20% of the basal ATPase activity of the wild type enzyme after 1 h incubation at 65°C
R155E
-
the mutant has severely diminished activity compared to the wild type enzyme
R155K
-
the mutant enzyme has about wild type activity
R155L
-
the mutant has severely diminished activity compared to the wild type enzyme
slou45
-
the ATPase activity of Hsp90 is abrogated by the slou45 mutation
A109C
the mutant is defective in ring separation and exchange
A109S
the mutant shows mixed-ring formation like the wild type enzyme
A399T
-
site-diretected mutagenesis, the mutation weakens the affinity for GroES by about 90fold
A92T
-
site-diretected mutagenesis, the mutation weakens the affinity for GroES by about 1600fold
C138S/C458S/C519S/D83C/K327C
conformational change, in reduced state similar ATP hydrolysis and ATP binding to wild-type GroEL
C138W
-
at 37°C, the mutant enzyme is indistinguishable in all aspects from the wild type, however, at 25°C, steric hindrances cause the chaperonin to be arrested in a ternary complex form, with both unfolded protein and GroES bound to the same ring of the enzyme. An increase in temperature to more than 30°C is sufficient to restart both target protein refolding and ATPase activity in the mutant enzyme
D115N
-
site-diretected mutagenesis, the mutation weakens the affinity for GroES by about 50fold
D155A
the mutant preserves negative inter-ring cooperativity and forms mixed-ring complexes in the presence of cofactor GroES/ATP with an efficiency similar to the wild type enzyme
D155A/R197A
the double mutant preserves negative inter-ring cooperativity and forms mixed-ring complexes in the presence of cofactor GroES/ATP with an efficiency similar to the wild type enzyme
D398K
block of ATP hydrolysis
D52A
-
site-directed mutagenesis, ATPase activity of the mutant is 80% reduced compared to the wild-type GroEL
D52A/D358A
ATPase-deficient mutant
D83A/R197A
allosterically compromised mutant
D87K
the mutant enzyme does not bind nucleotide
E191G
-
site-diretected mutagenesis, the mutation weakens the affinity for GroES by about 300fold
EL-2GGM4
-
cavity size mutant, cis-cavity volume 96%, net charge -42
EL-2GGM4-D398A
-
ATPase deficient mutant
EL-3GGM4
-
cavity size mutant, cis-cavity volume 91%, net charge -42
EL-3GGM4-D398A
-
ATPase deficient mutant
EL-3N3Q
-
charge mutant, cis-cavity volume 100%, net charge 0
EL-4GGM4
-
cavity size mutant, cis-cavity volume 87%, net charge -42
EL-KKK2
-
charge mutant, cis-cavity volume 100%, net charge 0
EL-NNQ
-
charge mutant, cis-cavity volume 100%, net charge -21
EL398A/D490C
conformational change, mutant of GroEL
ELDELTAC
-
cavity size mutant, cis-cavity volume 104%, net charge -42
F44W/E257A
-
the mutation E257A abolishes the nonfolded protein substrate binding-induced stimulation of ATPase activity
G192W
-
the mutant enzyme is capable of binding to GroES in the absence of ATP binding
K105A
allosterically compromised mutant
R231W
site-directed mutagenesis, apical domain mutation, slower phases following addition of ATP to tryptophan-modified GroEL mutant
Y199E
conformational change, reduced affinity for GroES
Y203E
conformational change, single mutation of GroEL
Y203E/G337S/I349E
the mutant enzyme is ATPase active but unable to bind substrate protein and the cofactor GroES
Y360F
conformational change, single mutation of GroEL
Y476F
conformational change, single mutation of GroEL
Y478F
conformational change, single mutation of GroEL
Y485F
conformational change, single mutation of GroEL
Y506E
conformational change, single mutation of GroEL
Y506W
conformational change, single mutation of GroEL
D155A
-
unconcerted release of substrate domains by ATP
F44W
-
unconcerted release of substrate domains by ATP
E315C
-
mutant of GroEL
-
C51A
-
wild-type HpGroES binds two Zn2+ per monomer. H45A, C51A, and C53A decrease to 0.3-0.5 Zn2+ per monomer
C51A/C53A
-
the double-cysteine mutant gives only 0.12 Zn2+ per monomer
C53A
-
wild-type HpGroES binds two Zn2+ per monomer. H45A, C51A, and C53A decrease to 0.3-0.5 Zn2+ per monomer
H45A
-
wild-type HpGroES binds two Zn2+ per monomer. H45A, C51A, and C53A decrease to 0.3-0.5 Zn2+ per monomer
G67S
-
additional wild-type control, because this variation is present in a Hsp60 cDNA clone
H147R
-
the mutation is associated with hereditary sensory neuropathies
V98I
-
mutation affects the ATPase activity and results in a dramatically decreased folding activity
D386A
-
in order to study the Mm-cpn in the ATP bound state, a lidless Mm-cpn variant (D386A DELTAlid Mm-cpn) is chosen. The mutation of Asp386 to an alanine makes the chaperonin ATPase deficient. This mutant can still bind but cannot hydrolyze ATP. Cryo-EM raw images and two-dimensional class-averages show D386A DELTAlid Mm-cpn is open in the ATP bound state as represented by rectangular-shaped side view and ring-shaped top view with clear subunit boundaries. This appears similar to those images of the D386A Mm-cpn without the lid deletion in the ATP-bound state
K256C
-
the mutant changes from the opened to closed conformation in an ATP-dependent manner
T327A/N328A/K330A/D331A
-
mutants achieve essentially the same closed state as the wild-type counterparts, mutants are competent for ATP binding and hydrolysis. Another mutant which in addition to the 4 Ala substitution lacks the entire lid-forming segments is incapable of releasing either substrate in the presence of ATP. This suggests that the lateral contacts between helix 11 and the rls loop 327-331 are important for releasing the substrate upon ATP hydrolysis
G346
-
mutation in CCTalpha causes defects in cilia and impaires CCTalpha localization in cilia
D545G
-
the mutant shows its highest activity at 60°C, with a value equal to that of wild type isoform CpkA
D545M
-
the optimal activity of the mutant is at 70°C, with a value equal to that of wild type isoform CpkA
E530G
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the mutant of isoform CpkA shows increased ATPase and protein refolding activities, with its highest activity at 50°C. The mutation prevents cold denaturation of proteins under cold stress conditions, thereby enabling cells to grow in cooler environments
E530M
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the mutant enzyme shows the most activity at 70°C, although the value is almost half that of wild type enzyme isoform CpkA. The ATPase activity of the mutant at 50°C is a little lower than that of the wild type enzyme
P533M
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the mutant shows optimal activity at 70°C, with a value similar to that of wild type isoform CpkA
P538G
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the mutant shows a temperature-dependent profile similar to that of wild type isoform CpkA, although its ATPase activity is almost 2fold lower
Q533G
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the mutant enzyme shows the most activity at 50°C, although the value is similar to that of the wild type enzyme isoform CpkA. The ATPase activity of the mutant at 50°C is a little lower than that of the wild type enzyme
Q533M
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the optimum activity of the enzyme is displayed at 80°C and is 4fold higher than that of wild type isoform CpkA at this temperature
E530G
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the mutant of isoform CpkA shows increased ATPase and protein refolding activities, with its highest activity at 50°C. The mutation prevents cold denaturation of proteins under cold stress conditions, thereby enabling cells to grow in cooler environments
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E530M
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the mutant enzyme shows the most activity at 70°C, although the value is almost half that of wild type enzyme isoform CpkA. The ATPase activity of the mutant at 50°C is a little lower than that of the wild type enzyme
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P538G
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the mutant shows a temperature-dependent profile similar to that of wild type isoform CpkA, although its ATPase activity is almost 2fold lower
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Q533G
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the mutant enzyme shows the most activity at 50°C, although the value is similar to that of the wild type enzyme isoform CpkA. The ATPase activity of the mutant at 50°C is a little lower than that of the wild type enzyme
-
Q533M
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the optimum activity of the enzyme is displayed at 80°C and is 4fold higher than that of wild type isoform CpkA at this temperature
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D393A
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impaired ATP hydrolysis activity
D64A
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impaired ATP hydrolysis activity
G65S
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20% decrease in ATPase activity
I125T
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same ATPase activity as wild-type
I125T/G65C
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mutant lacks ATP-dependent protein refolding activity, despite showing ATPase activity
trapalpha
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mutant, traps the unfolded and partially folded substrate protein
D393A
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impaired ATP hydrolysis activity
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D64A
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impaired ATP hydrolysis activity
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G65S
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20% decrease in ATPase activity
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I125T
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same ATPase activity as wild-type
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I125T/G65C
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mutant lacks ATP-dependent protein refolding activity, despite showing ATPase activity
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D391A
ATP, ADP, and AMP hydrolysis activities decreased significantly compared to wild type, with the exception of the ATP hydrolysis in presence of Co2+
D394A
ATP, ADP, and AMP hydrolysis activities decreased significantly compared to wild type
D62A
ATP, ADP, and AMP hydrolysis activities decreased significantly compared to wild type
D67A
ATP, ADP, and AMP hydrolysis activities decreased significantly compared to wild type, with the exception of the ATP hydrolysis in presence of Co2+
D93K
the mutation of the beta subunit blocks ATP hydrolysis. The mutant has 43% of wild type protein refolding activity
D94A
the mutation of the alpha subunit blocks ATP hydrolysis. The mutant has 32% of wild type protein refolding activity
D94K
the mutation of the alpha subunit blocks ATP hydrolysis. The mutant has 31% of wild type protein refolding activity
T157A
the mutation of the alpha subunit blocks ATP binding. The mutant has 30.5% of wild type protein refolding activity
T158A
the mutation of the beta subunit blocks ATP binding. The mutant has 62.6% of wild type protein refolding activity
T96V
the mutation of the beta subunit blocks ATP binding. The mutant has 44% of wild type protein refolding activity
T97V
the mutation of the alpha subunit blocks ATP binding. The mutant has no activity
D398A
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ATPase deficient mutant
D398A
conformational change, slow ATP hydrolysis
D398A
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to explore the multiple conformations induced upon ATP binding to GroEL a mutant is used. Mutant shows normal ATP binding but 3% of the wild-type steady-state ATPase activity. Statistical analysis of a large data set of single-particle cryo-EM images of mutant is carried out: multiple pre-hydrolysis conformations are resolved that can be ordered into a sequence to trace out smooth trajectories of domain movements for GroEL-ATP7 and GroEL-ATP14 complexes. The structures reveal a set of salt-bridge changes that provide a series of click stops (preferred conformations) on a trajectory to a conformation in which the apical domains are separated from each other and partially elevated but lack the full elevation and large clockwise twist seen in the GroES bound rings. This elevated, open conformation of the GroEL ring positions the GroES-binding sites on its apical surface, while still exposing key hydrophobic sites toward the cavity
D398A
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to measure the rate of ADP release from an asymmetric GroEL/GroES/ADP7 complex, D398A mutant is employed. The mutant hydrolyzes ATP at a rate 2% that of wild-type GroEL, and thus effectively allows study of a single turnover of the reaction
D398A
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site-directed mutagenesis, the mutant shows reduced ATPase activity compared to the wild-type enzyme
D398A
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ATP-hydrolysis deficient mutant
D398A
the mutant enzyme binds ATP but hydrolyzes it at a very slow rate of less than 2% of the wild type enzyme
D52A/D398A
site-directed mutagenesis
D52A/D398A
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site-directed mutagenesis, the mutant forms a stable symmetric GroEL-GroES complex with a half-life of 150 h, but has no ATPase activity
E315C
site-directed mutagenesis
E461K
site-directed mutagenesis, the inactive mutant of GroEL has a rearranged inter-ring interface, the normal 1:2 contacts of apposed equatorial domains in wild-type GroEL are replaced by 1:1 contacts in the mutant in the interfaces
E461K
the mutant enzyme shows no mixed-ring formation
F44W
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wild-type variant in which the F44W mutation is introduced so that ATP-induced conformation changes can be followed by monitoring time-resolved changes in fluorescence
F44W
site-directed mutagenesis, slower phases following addition of ATP to tryptophan-modified GroEL mutant
I493C
mutation in binding pocket of GroEL
I493C
-
normal ATP hydrolysis in absence of inhibitor
Y485W
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mutant is used in this study to monitor the MgATP2-binding process to unliganded apo GroEL in the absence of K+ at pH 7.5 and 5.1°C. Under these conditions ATP exists mostly as MgATP2- and [MgATP2-]
Y485W
site-directed mutagenesis, equatorial ring mutation, slower phases following addition of ATP to tryptophan-modified GroEL mutant
G345D
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mutation in subunit CCT4, located in the external region of the apical domain, causes actin defects in the temperature-sensitive yeast strain anc2-1. Using the spectroscopic folding assay, the rate of release of AcrylAct1 by CCT4anc2 is found to be essentially the same as for wild-type CCT at 2 mM ATP but different at higher concentrations
G345D
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the mutation in subunit CCT4 decreases cooperativity in ATP binding
G65C
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same ATPase activity as wild-type
G65C
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impaired ATP-dependent conformational change ability
G65C
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same ATPase activity as wild-type
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G65C
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impaired ATP-dependent conformational change ability
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additional information
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used in complex with gp23 and gp31 of bacteriophage T4
additional information
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construction of a single-ring GroELSR. GroELSRA399T-GroES and GroELSRD115N-GroES single-ring systems support cell growth in the same manner as the wild-type double-ring GroELeGroES at 37°C and 42°C, while mutant GroELSRA92T-GroES complements GroEL-GroES at both 37°C and 42°C, and mutant GroELSRE191G-GroES complements GroEL-GroES to a lesser extent at 37°C, but not at 42°C. Activities of functional single-ring GroELSReGroES system mutants, overview
additional information
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the refolding of urea-denatured rhodanese is catalzed at low temperatures by oxidized GroEL, which contains increased exposed hydrophobic surfaces and retains its ability to hydrolyse ATP, oxidation of GroEL with H2O2. Oxidized GroEL efficiently binds the urea-unfolded rhodanese at 4°C, without requiring excess amount of chaperonin relative to normal GroEL (i.e. non-oxidized). The oxidized GroEL has the potential to efficiently trap recombinant or non-native proteins at 4°C and release them at higher temperatures under appropriate conditions
additional information
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wild-type HpGroES binds two Zn2+ per monomer, HpGroESDELTAMBD (MBD i.e. metalbinding domain) contains 0.71 per monomer
additional information
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a lid variant is created that lacks the entire lid-forming segments: variant achieves the same ATP-induced closed conformation as wild-type, ATPase activity and substrate-binding ability are unaffected, substrate release from mutant cannot be ascribed to completion of folding
additional information
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identical mutations in the different CCT subunits lead to different phenotypes. Mutation in subunit CCT2 displays heat sensitivity and cold sensitivity for growth, have an excess of actin patches, and are the only strain here generated that is pseudo-diploid. Cells with the mutation in subunit CCT7 are the only ones to accumulate juxtanuclear protein aggregates that may reflect an impaired stress response in this strain
additional information
Tequatrovirus T4
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used in complex with gp23 of bacteriophage T4 and GroEL of Escherichia coli
additional information
Tequatrovirus T4
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used in complex with gp31 of bacteriophage T4 and GroEL of Escherichia coli
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