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Information on EC 5.6.1.7 - chaperonin ATPase and Organism(s) Escherichia coli and UniProt Accession P0A6F5

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IUBMB Comments
Multisubunit proteins with 2x7 (Type I, in most cells) or 2x8 (Type II, in Archaea) ATP-binding sites involved in maintaining an unfolded polypeptide structure before folding or entry into mitochondria and chloroplasts. Molecular masses of subunits ranges from 10-90 kDa. They are a subclass of molecular chaperones that are related to EC 5.6.1.5 (proteasome ATPase).
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This record set is specific for:
Escherichia coli
UNIPROT: P0A6F5
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The taxonomic range for the selected organisms is: Escherichia coli
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
hide
ATP
+
H2O
+
a folded polypeptide
=
ADP
+
phosphate
+
an unfolded polypeptide
+
+
a folded polypeptide
=
+
+
an unfolded polypeptide
Synonyms
chaperonin, hsp65, groes, heat shock protein 60, cpn60, hsp10, cpn10, chaperonin groel, chaperonin 60, groel2, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
bacterial chaperonin
-
-
chaperonin
chaperonin ATPase
-
-
chaperonin GroEL
-
-
chaperonin GroEL/ES
-
-
co-chaperonin GroES
-
-
GroEl
GroEL ATPase
-
-
GroEL chaperonin
-
-
GroEL-GroES
-
-
GroEL/GroES
-
-
group I chaperonin
-
-
SR1-GroEL
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
ATP + H2O + a folded polypeptide = ADP + phosphate + an unfolded polypeptide
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hydrolysis
hydrolysis of phosphoric ester
-
-
hydrolysis of phosphonic ester
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
ATP phosphohydrolase (polypeptide-unfolding)
Multisubunit proteins with 2x7 (Type I, in most cells) or 2x8 (Type II, in Archaea) ATP-binding sites involved in maintaining an unfolded polypeptide structure before folding or entry into mitochondria and chloroplasts. Molecular masses of subunits ranges from 10-90 kDa. They are a subclass of molecular chaperones that are related to EC 5.6.1.5 (proteasome ATPase).
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
show the reaction diagram
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
show the reaction diagram
ATP + H2O + folded 5(6)-carboxytetramethylrhodamine-tagged bacteriorhodopsin peptide
ADP + phosphate + unfolded 5(6)-carboxytetramethylrhodamine-tagged bacteriorhodopsin peptide
show the reaction diagram
-
i.e. 5(6)-carboxytetramethylrhodamine-KKAITTLVPAIAFTMYLSMLLKK
-
-
?
additional information
?
-
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
show the reaction diagram
ATP + H2O + a folded polypeptide
ADP + phosphate + an unfolded polypeptide
show the reaction diagram
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
GroES
-
GroES
-
additional information
-
GroES encapsulates substrate protein
-
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ca2+
-
is found to protect against proteolysis of a form of GroEL, ox-GroEL, prepared by exposing GroEL to hydroxide peroxide, induces a conformational change
Co2+
-
2 mM, 41% of activity with Mg2+
NH4+
-
can fully substitute for K+
Zn2+
-
is found to protect against proteolysis of a form of GroEL, ox-GroEL, prepared by exposing GroEL to hydroxide peroxide, induces a conformational change
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
EC3016
inhibits ATPase activity of mutant I493C
ADP
-
more than 80% inhibition at 10fold excess of ADP
EDTA
-
removing of Mg2+, complete inhibition
GroES
-
Guanidinium chloride
-
20% inhibition with 150 mM guanidinium chloride in the presence of 100 mM KCl, 80% inhibition with 1 mM KCl
MgADP
-
50% inhibition at 0.205 mM
Mn2+
-
25% reversible inhibition of Mg-ATPase activity
MnADP
-
50% inhibition at 0.036 mM
N-[4-(4-amino-1-tert-butyl-1H-pyrazolo[3,4-d]pyrimidin-3-yl)phenyl]cyclopentanecarboxamide
-
specifically blocks ATP binding and hydrolysis
NaCl
-
50% inhibition with 150 mM
yeast mitochondrial chaperonin hsp10
-
40% inhibition of GroEL at 25 and 30°C
-
additional information
physiological ADP concentration suppresses formation of symmetric complexes
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
ATP
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
GroES
an allosteric effector of ATP hydrolysis. GroES contact leads to large rigid-body apical movements that eject polypeptide into an enclosed folding chamber. Docking of GroES stabilizes the Rs-open state, taking this assembly to a more energetically stable state that is no longer reversible and that is committed to the further large movements to a final energetic minimum that is the fully domed end state
-
GroES
-
N-ethylmaleimide
-
2fold increase in activity after modification of GroEL with 2 mM N-ethylmaleimide
unfolded substrate protein
-
chaperonin machine enhances hemicycle time and mean residence time set by the rate of ATP hydrolysis by the cis ring
-
additional information
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.007
ATP
-
50 mM K+
additional information
additional information
-
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.025 - 0.75
ATP
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
0.751
-
at 37°C
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.8
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
22
-
ATPase activity assay at room temperature
22 - 37
-
release/reactivation of rhodanese from/by GroEL
23
-
assay at
49
-
in the presence of 2 mM K+ and Mg2+
5
-
assay at
additional information
-
assay at 24°C
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25 - 60
-
approx. 50% of maximal activity at 30°C, approx. 90% of maximal activity at 55°C, almost no activity at 60°C
25 - 64
-
ATPase activity gradually increases between 25°C and 52°C, strong decrease above
25 - 70
-
approx. 15% of maximal activity at 40°C, approx. 20% of maximal activity at 68°C
4 - 37
-
and above, the release/reactivation of rhodanese from/by GroEL is minimal at 4°C, but is optimal between 22°C and 37°C
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
evolution
malfunction
-
a wider range of newly synthesized proteins aggregated upon rapid loss of GroEL function in a temperature-sensitive GroEL mutant strain. Most GroEL interactors are 35-60 kDa in size, consistent with the volume of the GroEL-GroES cavity. Role of chaperonin in evolution, overview
metabolism
the enzyme helps protein folding by undergoing a conformational change from a closed state to an open state
physiological function
additional information
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
57000
14 * 57000
57000
57259
-
x * 57259, sequence calculation, x * 60000, recombinant enzyme, SDS-PAGE
57260
-
monomer
58000
-
14 * 58000, two heptameric rings stacked back-to-back
60000
800000
-
GroEL, two stacked heptameric rings of 57 kDa subunits
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
tetradecamer
?
-
x * 57259, sequence calculation, x * 60000, recombinant enzyme, SDS-PAGE
heptamer
homotetradecamer
oligomer
tetradecamer
additional information
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
analysis of the X-ray crystal structures of GroEL and GroEL-GroES complexes in absence or presence of ATP, PDB IDs 1OEL and 1SVT, and of enzyme mutant E461K interface, PDB ID 2EU1
analysis of crystal structures of the GroE chaperonin from Escherichia coli in the open, ATP-bound, PDB ID 1KP8, and closed, PDB ID 1AON, states
-
crystals of GroELE461K are grown at 4°C in hanging-drop vapour-diffusion experiments. The crystal structure of the mutant chaperonin GroELE461K is determined at 3.3 A and compared with other structures
-
frozen-hydrated GroEL complexes, 30A resolution, 7fold symmetry, two interring contacts per subunit, ATP turnover causes allosteric switching between the rings by altering the interring contacts
-
sitting-drop vapour-diffusion method. The well solution contains 100 mM Na-Hepes (pH 7.5), 20% (w/v) PEG 4000, 200 mM (NH4)2SO4. Concentration of protein in a drop, after mixing with an equal volume of precipitant solution, is 15–20 mg/ml. Crystals appears after one week at 18°C
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
A109C
the mutant is defective in ring separation and exchange
A109S
the mutant shows mixed-ring formation like the wild type enzyme
C138S/C458S/C519S/D83C/K327C
conformational change, in reduced state similar ATP hydrolysis and ATP binding to wild-type GroEL
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
D398A
D398K
block of ATP hydrolysis
D52A/D358A
ATPase-deficient mutant
D52A/D398A
site-directed mutagenesis
D83A/R197A
allosterically compromised mutant
D87K
the mutant enzyme does not bind nucleotide
E315C
site-directed mutagenesis
E461K
EL398A/D490C
conformational change, mutant of GroEL
F44W
site-directed mutagenesis, slower phases following addition of ATP to tryptophan-modified GroEL mutant
I493C
mutation in binding pocket of GroEL
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
Y485W
site-directed mutagenesis, equatorial ring mutation, slower phases following addition of ATP to tryptophan-modified GroEL mutant
Y506E
conformational change, single mutation of GroEL
Y506W
conformational change, single mutation of GroEL
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
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
D398A
D52A
-
site-directed mutagenesis, ATPase activity of the mutant is 80% reduced compared to the wild-type GroEL
D52A/D398A
-
site-directed mutagenesis, the mutant forms a stable symmetric GroEL-GroES complex with a half-life of 150 h, but has no ATPase activity
E191G
-
site-diretected mutagenesis, the mutation weakens the affinity for GroES by about 300fold
E315C
-
mutant of GroEL
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
ELDELTAC
-
cavity size mutant, cis-cavity volume 104%, net charge -42
F44W
-
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/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
I493C
-
normal ATP hydrolysis in absence of inhibitor
Y485W
-
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-]
additional information
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35
-
half-life at 70°C, 30 min, less than 5% activity retained after 90 min
43
-
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 GroEL–rhodanese 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
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
GroEL is rather insensitive to oxidants produced endogenously during metabolism, such as nitric oxide or hydrogen peroxide, but is efficiently modified and inactivated by reactive species generated by phagocytes, such as peroxynitrite and hypochlorous acid (HOCl). HOCl inactivates through the oxidation of methionine to methionine sulfoxide. In addition to the oxidation of methionine, HOCl causes the conversion of cysteine to cysteic acid and this product may account for the remainder of inactivated GroEL not recoverable through MsrB/A. HOCl produces only negligible yields of 3-chlorotyrosine. The high sensitivity of GroEL toward HOCl and ONOO suggests that this protein may be a target for bacterial killing by phagocytes
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant GroEL wild-type and mutants from Escherichia coli strain BL21(DE3)
ammonium sulfate precipitation
-
GroEL is purified from lysates of Escherichia coli bearing the multicopy plasmid pGroESL
-
HiTrap Q Sepharose column chromatography
-
more than 95% pure after SDS-PAGE
-
recombinant chaperonin GroEL from Escherichia coli
-
recombinant GroEL
-
Sephacryl S-300, Q-Sepharose
-
using two ion-exchange dimensions followed by gel filtration
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cloning of GroEL wild-type and mutants in Escherichia coli strain DH5alpha, recombinant expression in Escherichia coli strain BL21(DE3), co-expression with cofactor GroES
expression in Escherichia coli
expressed in Escherichia coli BL21(DE3) cells
-
expression in Escherichia coli
-
expression in Escherichia coli BL21
-
full-length wild-type E. coli GroEL is expressed in Escherichia coli strain W3110 bearing a multicopy of the noninducible pOF39 plasmid
-
GroEL in pTRC99a is overexpressed in Escherichia coli DH5alpha cells
-
GroEL mutants are constructed in a pCH vector backbone, chaperonin constructs for in vivo co-expression are prepared by inserting the fragments into the pOFXtac-SL2 vector, furthermore the vectors pCH-L16-GFP and pBAD18 are used
-
into the pET24d vector for expression in Escherichia coli BL21DE3 cells
-
recombinant expression of chaperonin GroEL in Escherichia coli cells bearing the multicopy plasmid pGroESL
-
the N-cpn20 and C-cpn20 homologs of mature wild type cpn20 are cloned individually into the pGEM T-easy vector, the constructs are further cloned into pET22b+
-
wild type and mutant D490C enzymes are expressed in Escherichia coli XL1-Blue cells
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
GroEL/GroES overexpression doubles the number of accumulating mutations, and promotes the folding of enzyme variants carrying mutations in the protein core and/or mutations with higher destabilizing effects
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Higurashi, T.; Nosaka, K.; Mizobata, T.; Nagai, J.; Kawata, Y.
Unfolding and refolding of Escherichia coli chaperonin GroES is expressed by a three-state model
J. Mol. Biol.
291
703-713
1999
Escherichia coli
Manually annotated by BRENDA team
Martin, J.
Role of the GroEL chaperonin intermediate domain in coupling ATP hydrolysis to polypeptide release
J. Biol. Chem.
273
7351-7357
1998
Escherichia coli
Manually annotated by BRENDA team
Ranson, N.A.; White, H.E.; Saibil, H.R.
Chaperonins
Biochem. J.
333
233-242
1998
Escherichia coli
Manually annotated by BRENDA team
Dubaquie, Y.; Loosers, R.; Rospert, S.
Significance of chaperonin 10-mediated inhibition of ATP hydrolysis by chaperonin 60
Proc. Natl. Acad. Sci. USA
94
9011-9016
1997
Saccharomyces cerevisiae, Escherichia coli
Manually annotated by BRENDA team
Mendoza, J.A.; Warren, T.; Dulin, P.
The ATPase activity of chaperonin GroEL is highly stimulated at elevated temperatures
Biochem. Biophys. Res. Commun.
229
271-274
1996
Escherichia coli
Manually annotated by BRENDA team
Cross, S.J.; Cirulea, A.; Poomputsa, K.; Romaniec, M.P.; Freedman, R.B.
Thermostable chaperonin from Clostridium thermocellum
Biochem. J.
316
615-622
1996
Acetivibrio thermocellus, Escherichia coli
Manually annotated by BRENDA team
Roseman, A.M.; Chen, S.; White, H.; Braig, K.; Saibil, H.R.
The chaperonin ATPase cycle: mechanism of allosteric switching and movements of substrate-binding domains in GroEL
Cell
87
241-251
1996
Escherichia coli
Manually annotated by BRENDA team
Diamant, S.; Azem, A.; Weiss, C.; Gouloubinoff, P.
Effect of free and ATP-bound magnesium and manganese ions on the ATPase activity of chaperonin GroEL
Biochemistry
34
273-277
1995
Escherichia coli
Manually annotated by BRENDA team
Todd, M.J.; Lorimer, G.H.
Stability of the asymmetric Escherichia coli chaperonin complex
J. Biol. Chem.
270
5388-5394
1995
Escherichia coli
Manually annotated by BRENDA team
Yifrach, O.; Horovitz, A.
Nested cooperativity in the ATPase activity of the oligomeric chaperonin GroEL
Biochemistry
34
5303-5308
1995
Escherichia coli
Manually annotated by BRENDA team
Todd, M.J.; Viitanen, P.V.; Lorimer, G.H.
Dynamics of the cochaperonin ATPase cycle: implications for facilitated protein folding
Science
265
659-666
1994
Escherichia coli
Manually annotated by BRENDA team
Terlesky K.C.; Tabita, F.R.
Purification and characterization of the chaperonin 10 and chaperonin 60 proteins from Rhodobacter sphaeroides
Biochemistry
30
8181-8186
1991
Escherichia coli, Cereibacter sphaeroides
Manually annotated by BRENDA team
Viitanen, P.V.; Lubben, T.H.; Reed, J.; Goloubinoff, P.; O'Keefe, D.P.; Lorimer, G.H.
Chaperonin-facilitated refolding of ribulosebisphosphate carboxylase and ATP hydrolysis by chaperonin 60 (groel) are K+ dependent
Biochemistry
29
5665-5671
1990
Escherichia coli
Manually annotated by BRENDA team
George, R.; Kelly, S.M.; Price, N.C.; Erbse, A.; Fisher, M.; Lund, P.A.
Three GroEL homologues from Rhizobium leguminosarum have distinct in vitro properties
Biochem. Biophys. Res. Commun.
324
822-828
2004
Escherichia coli, Rhizobium leguminosarum
Manually annotated by BRENDA team
Inobe, T.; Makio, T.; Takasu-Ishikawa, E.; Terada, T.P.; Kuwajima, K.
Nucleotide binding to the chaperonin GroEL: non-cooperative binding of ATP analogs and ADP, and cooperative effect of ATP
Biochim. Biophys. Acta
1545
160-173
2001
Escherichia coli
Manually annotated by BRENDA team
Melkani, G.C.; Zardeneta, G.; Mendoza, J.A.
The ATPase activity of GroEL is supported at high temperatures by divalent cations that stabilize its structure
BioMetals
16
479-484
2003
Escherichia coli
Manually annotated by BRENDA team
Chaudhuri, T.K.; Gupta, P.
Factors governing the substrate recognition by GroEL chaperone: a sequence correlation approach
Cell Stress Chaperones
10
24-36
2005
Escherichia coli
Manually annotated by BRENDA team
Melkani, G.C.; Zardeneta, G.; Mendoza, J.A.
On the chaperonin activity of GroEL at heat-shock temperature
Int. J. Biochem. Cell Biol.
37
1375-1385
2005
Escherichia coli
Manually annotated by BRENDA team
van Duijn, E.; Simmons, D.A.; van den Heuvel, R.H.; Bakkes, P.J.; van Heerikhuizen, H.; Heeren, R.M.; Robinson, C.V.; van der Vies, S.M.; Heck, A.J.
Tandem mass spectrometry of intact GroEL-substrate complexes reveals substrate-specific conformational changes in the trans ring
J. Am. Chem. Soc.
128
4694-4702
2006
Escherichia coli
Manually annotated by BRENDA team
Khor, H.K.; Fisher, M.T.; Schoeneich, C.
Potential role of methionine sulfoxide in the inactivation of the chaperone GroEL by hypochlorous acid (HOCl) and peroxynitrite(ONOO-)
J. Biol. Chem.
279
19486-19493
2004
Escherichia coli
Manually annotated by BRENDA team
Chaudhry, C.; Horwich, A.L.; Brunger, A.T.; Adams, P.D.
Exploring the structural dynamics of the E. coli chaperonin GroEL using translation-libration-screw crystallographic refinement of intermediate states
J. Mol. Biol.
342
229-245
2004
Escherichia coli
Manually annotated by BRENDA team
Bartolucci, C.; Lamba, D.; Grazulis, S.; Manakova, E.; Heumann, H.
Crystal structure of wild-type chaperonin GroEL
J. Mol. Biol.
354
940-951
2005
Escherichia coli
Manually annotated by BRENDA team
Cabo-Bilbao, A.; Spinelli, S.; Sot, B.; Agirre, J.; Mechaly, A.E.; Muga, A.; Guerin, D.M.
Crystal structure of the temperature-sensitive and allosteric-defective chaperonin GroELE461K
J. Struct. Biol.
155
482-492
2006
Escherichia coli
Manually annotated by BRENDA team
Jones, H.; Preuss, M.; Wright, M.; Miller, A.D.
The mechanism of GroEL/GroES folding/refolding of protein substrates revisited
Org. Biomol. Chem.
4
1223-1235
2006
Escherichia coli
Manually annotated by BRENDA team
Horst, R.; Bertelsen, E.B.; Fiaux, J.; Wider, G.; Horwich, A.L.; Wuethrich, K.
Direct NMR observation of a substrate protein bound to the chaperonin GroEL
Proc. Natl. Acad. Sci. USA
102
12748-12753
2005
Escherichia coli
Manually annotated by BRENDA team
Panda, M.; Horowitz, P.M.
Activation parameters for the spontaneous and pressure-induced phases of the dissociation of single-ring GroEL (SR1) chaperonin
Protein J.
23
85-94
2004
Escherichia coli
Manually annotated by BRENDA team
Melkani, G.C.; Sielaff, R.L.; Zardeneta, G.; Mendoza, J.A.
Divalent cations stabilize GroEL under conditions of oxidative stress
Biochem. Biophys. Res. Commun.
368
625-630
2008
Escherichia coli
Manually annotated by BRENDA team
Tang, Y.C.; Chang, H.C.; Chakraborty, K.; Hartl, F.U.; Hayer-Hartl, M.
Essential role of the chaperonin folding compartment in vivo
EMBO J.
27
1458-1468
2008
Escherichia coli
Manually annotated by BRENDA team
Bonshtien, A.L.; Weiss, C.; Vitlin, A.; Niv, A.; Lorimer, G.H.; Azem, A.
Significance of the N-terminal domain for the function of chloroplast cpn20 chaperonin
J. Biol. Chem.
282
4463-4469
2007
Escherichia coli
Manually annotated by BRENDA team
Bross, P.; Naundrup, S.; Hansen, J.; Nielsen, M.N.; Christensen, J.H.; Kruh?ffer, M.; Palmfeldt, J.; Corydon, T.J.; Gregersen, N.; Ang, D.; Georgopoulos, C.; Nielsen, K.L.
The Hsp60-(p.V98I) mutation associated with Hereditary Spastic Paraplegia SPG13 compromises chaperonin function both in vitro and in vivo
J. Biol. Chem.
283
15694-15700
2008
Escherichia coli, Homo sapiens
Manually annotated by BRENDA team
Danziger, O.; Shimon, L.; Horovitz, A.
Glu257 in GroEL is a sensor involved in coupling polypeptide substrate binding to stimulation of ATP hydrolysis
Protein Sci.
15
1270-1276
2006
Escherichia coli
Manually annotated by BRENDA team
Chapman, E.; Farr, G.W.; Furtak, K.; Horwich, A.L.
A small molecule inhibitor selective for a variant ATP-binding site of the chaperonin GroEL
Bioorg. Med. Chem. Lett.
19
811-813
2009
Escherichia coli (P0A6F5)
Manually annotated by BRENDA team
Li, Y.; Gao, X.; Chen, L.
GroEL Recognizes an amphipathic helix and binds to the hydrophobic side
J. Biol. Chem.
284
4324-4331
2009
Escherichia coli
Manually annotated by BRENDA team
Tehver, R.; Thirumalai, D.
Kinetic model for the coupling between allosteric transitions in GroEL and substrate protein folding and aggregation
J. Mol. Biol.
377
1279-1295
2008
Escherichia coli
Manually annotated by BRENDA team
Clare, D.K.; Bakkes, P.J.; van Heerikhuizen, H.; van der Vies, S.M.; Saibil, H.R.
Chaperonin complex with a newly folded protein encapsulated in the folding chamber
Nature
457
107-110
2009
Tequatrovirus T4, Escherichia coli
Manually annotated by BRENDA team
Grason, J.P.; Gresham, J.S.; Lorimer, G.H.
Setting the chaperonin timer: a two-stroke, two-speed, protein machine
Proc. Natl. Acad. Sci. USA
105
17339-17344
2008
Escherichia coli, Escherichia coli JM105
Manually annotated by BRENDA team
Chapman, E.; Farr, G.W.; Fenton, W.A.; Johnson, S.M.; Horwich, A.L.
Requirement for binding multiple ATPs to convert a GroEL ring to the folding-active state
Proc. Natl. Acad. Sci. USA
105
19205-19210
2008
Escherichia coli
Manually annotated by BRENDA team
Chaudhuri, T.K.; Verma, V.K.; Maheshwari, A.
GroEL assisted folding of large polypeptide substrates in Escherichia coli: Present scenario and assignments for the future
Prog. Biophys. Mol. Biol.
99
42-50
2009
Escherichia coli
Manually annotated by BRENDA team
Hosono, K.; Ueno, T.; Taguchi, H.; Motojima, F.; Zako, T.; Yoshida, M.; Funatsu, T.
Kinetic analysis of conformational changes of GroEL based on the fluorescence of tyrosine 506
Protein J.
27
461-468
2008
Escherichia coli (P0A6F5)
Manually annotated by BRENDA team
Kim, S.Y.; Miller, E.J.; Frydman, J.; Moerner, W.E.
Action of the chaperonin GroEL/ES on a non-native substrate observed with single-molecule FRET
J. Mol. Biol.
401
553-563
2010
Escherichia coli
Manually annotated by BRENDA team
Tokuriki, N.; Tawfik, D.S.
Chaperonin overexpression promotes genetic variation and enzyme evolution
Nature
459
668-673
2009
Escherichia coli
Manually annotated by BRENDA team
Clare, D.K.; Vasishtan, D.; Stagg, S.; Quispe, J.; Farr, G.W.; Topf, M.; Horwich, A.L.; Saibil, H.R.
ATP-triggered conformational changes delineate substrate-binding and -folding mechanics of the GroEL chaperonin
Cell
149
113-123
2012
Escherichia coli
Manually annotated by BRENDA team
Tyagi, N.K.; Fenton, W.A.; Horwich, A.L.
ATP-triggered ADP release from the asymmetric chaperonin GroEL/GroES/ADP7 is not the rate-limiting step of the GroEL/GroES reaction cycle
FEBS Lett.
584
951-953
2010
Escherichia coli
Manually annotated by BRENDA team
Illingworth, M.; Ramsey, A.; Zheng, Z.; Chen, L.
Stimulating the substrate folding activity of a single ring GroEL variant by modulating the cochaperonin GroES
J. Biol. Chem.
286
30401-30408
2011
Escherichia coli
Manually annotated by BRENDA team
Chen, J.; Makabe, K.; Nakamura, T.; Inobe, T.; Kuwajima, K.
Dissecting a bimolecular process of MgATP2- binding to the chaperonin GroEL
J. Mol. Biol.
410
343-356
2011
Escherichia coli
Manually annotated by BRENDA team
Illingworth, M.; Salisbury, J.; Li, W.; Lin, D.; Chen, L.
Effective ATPase activity and moderate chaperonin-cochaperonin interaction are important for the functional single-ring chaperonin system
Biochem. Biophys. Res. Commun.
466
15-20
2015
Escherichia coli
Manually annotated by BRENDA team
Melkani, G.C.; Sielaff, R.; Zardeneta, G.; Mendoza, J.A.
Interaction of oxidized chaperonin GroEL with an unfolded protein at low temperatures
Biosci. Rep.
32
299-303
2012
Escherichia coli
Manually annotated by BRENDA team
Skjaerven, L.; Cuellar, J.; Martinez, A.; Valpuesta, J.M.
Dynamics, flexibility, and allostery in molecular chaperonins
FEBS Lett.
589
2522-2532
2015
Escherichia coli
Manually annotated by BRENDA team
Koike-Takeshita, A.; Mitsuoka, K.; Taguchi, H.
Asp-52 in combination with Asp-398 plays a critical role in ATP hydrolysis of chaperonin GroEL
J. Biol. Chem.
289
30005-30011
2014
Escherichia coli
Manually annotated by BRENDA team
Saibil, H.R.; Fenton, W.A.; Clare, D.K.; Horwich, A.L.
Structure and allostery of the chaperonin GroEL
J. Mol. Biol.
425
1476-1487
2013
Escherichia coli (P0A6F5)
Manually annotated by BRENDA team
Haldar, S.; Gupta, A.J.; Yan, X.; Milicic, G.; Hartl, F.U.; Hayer-Hartl, M.
Chaperonin-assisted protein folding: relative population of asymmetric and symmetric GroEL:GroES complexes
J. Mol. Biol.
427
2244-2255
2015
Escherichia coli (P0A6F5)
Manually annotated by BRENDA team
Dalton, K.M.; Frydman, J.; Pande, V.S.
The dynamic conformational cycle of the group I chaperonin C-termini revealed via molecular dynamics simulation
PLoS ONE
10
e0117724
2015
Escherichia coli
Manually annotated by BRENDA team
Hayer-Hartl, M.; Bracher, A.; Hartl, F.U.
The GroEL-GroES chaperonin machine: a nano-cage for protein folding
Trends Biochem. Sci.
41
62-76
2016
Escherichia coli
Manually annotated by BRENDA team
Suzuki, Y.; Yura, K.
Conformational shift in the closed state of GroEL induced by ATP-binding triggers a transition to the open state
Biophys. Physicobiol.
13
127-134
2016
Escherichia coli (Q548M1)
Manually annotated by BRENDA team
Mizobata, T.; Kawata, Y.
The versatile mutational repertoire of Escherichia coli GroEL, a multidomain chaperonin nanomachine
Biophys. Rev.
10
631-640
2018
Escherichia coli
Manually annotated by BRENDA team
Yan, X.; Shi, Q.; Bracher, A.; Milicic, G.; Singh, A.K.; Hartl, F.U.; Hayer-Hartl, M.
GroEL ring separation and exchange in the chaperonin reaction
Cell
172
605-617.e11
2018
Escherichia coli (P0A6F5)
Manually annotated by BRENDA team
Molugu, S.K.; Li, J.; Bernal, R.A.
Separation of E. coli chaperonin groEL from beta-galactosidase without denaturation
J. Chromatogr. B Analyt. Technol. Biomed. Life Sci.
1007
93-99
2015
Escherichia coli
Manually annotated by BRENDA team
Yamamoto, D.; Ando, T.
Chaperonin GroEL-GroES functions as both alternating and non-alternating engines
J. Mol. Biol.
428
3090-3101
2016
Escherichia coli
Manually annotated by BRENDA team
Lorimer, G.H.; Fei, X.; Ye, X.
The GroEL chaperonin a protein machine with pistons driven by ATP binding and hydrolysis
Philos. Trans. R. Soc. Lond. B Biol. Sci.
373
20170179
2018
Escherichia coli (P0A6F5)
Manually annotated by BRENDA team
Wang, X.; Chen, H.; Lu, X.; Chi, H.; Li, S.; Huang, F.
Probing the interaction mechanisms between transmembrane peptides and the chaperonin GroEL with fluorescence anisotropy
Spectrochim. Acta A.Mol. Biomol. Spectrosc.
194
1-7
2018
Escherichia coli
Manually annotated by BRENDA team
Boshoff, A.
Chaperonin-co-chaperonin interactions
Subcell. Biochem.
78
153-178
2015
Escherichia coli
Manually annotated by BRENDA team