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3.6.4.10: non-chaperonin molecular chaperone ATPase

This is an abbreviated version!
For detailed information about non-chaperonin molecular chaperone ATPase, go to the full flat file.

Word Map on EC 3.6.4.10

Reaction

ATP
+
H2O
=
ADP
 +
phosphate

Synonyms

70 kD heat shock protein, 90 kDa heat shock protein, 90-kDa heat shock protein, AAA+ ATPase, AAA+ ATPase ClpB, AAA+ chaperone, AAA+ chaperone ClpB, ATP-dependent foldase, ATPase, ATPase chaperone, ATPase ClpB, bATPase, BiP, bona fide chaperone, chaperone ClpB, chaperone hsp90, chaperone Hsp90alpha, chaperone Hsp90beta, ClpB, ClpB ATPase, ClpB chaperone, ClpB disaggregase, ClpB1, ClpB2, ClpB2/HSP101, ClpC, ClpC chaperone, ClpX, ClpX heat-shock protein, disaggregase, DnaK, DnaK ATPase, DnaK chaperone, endoplasmic reticulum chaperone, ER lumenal hsc70 BiP, eukaryotic Hsc70 ATPase, GroEl, GRP75, Grp78, hATPase, heat shock cognate 70, heat shock cognate protein, heat shock protein, heat shock protein 70, heat shock protein 90, heat shock protein 90-alpha, heat shock protein GroEl, heat shock protein-70, heat shock protein-90, heat-shock cognate protein 70, heat-shock protein 70, heat-shock protein 90, Hsc66, Hsc70, Hsc82, Hsp100, HSP101, Hsp104, Hsp14.0, Hsp19.7, Hsp40, Hsp60, Hsp70, Hsp70 chaperone, Hsp70 chaperone Ssa1, Hsp70-1, Hsp70-2, Hsp70-3, HSP70.1, HSP70.2, Hsp82, Hsp82p, Hsp90, Hsp90 molecular chaperone, Hsp90a, Hsp90alpha, HSPA1L, HspA8, HspA9, HtpG, human alphabeta crystallin, human Hsp70 molecular chaperone, human stress70c, inducible heat shock protein 70, Kar2, maize stress70er, MecB protein, mitochondrial chaperone, mitochondrial heat shock protein 40, mitochondrial heat shock protein 70, mitochondrial heat-shock protein 70, mitochondrial hsp70, molecular chaperone, molecular chaperone BiP, molecular chaperone GroEl, molecular chaperone Hsc70 ATPase, mortalin, mortalin/mtHsp70, mouse alphabeta crystallin, mtHsp40, mtHSP70, p97-valosin-containing protein, p97-VCP, PBP74, PfClpB1, PfHsp70, PoHsp70, Pt-Hsp70, Ssq1, stress70 protein, SyClpC, tomato stress70c, vacuolar H+-ATPase, vacuolar membrane ATPase, yHsp90

ECTree

     3 Hydrolases
         3.6 Acting on acid anhydrides
             3.6.4 Acting on acid anhydrides to facilitate cellular and subcellular movement
                3.6.4.10 non-chaperonin molecular chaperone ATPase

Crystallization

Crystallization on EC 3.6.4.10 - non-chaperonin molecular chaperone ATPase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
44-kDa wild-type Hsc70 ATPase fragment
-
hanging-drop vapour-diffusion method. Crystals of the C-terminal 10 kDa helical lid domain (residues 542–640) from a Caenorhabditis elegans Hsp70 homologue, diffract X-rays to 3.4 A, crystals belong to space group I2(1)2(1)2(1), with unit-cell parameters a = b = 197, c = 200 A
-
crystals of ClpB diffract to 1.95 A
-
crystals of ClpB nucleotide-binding domain 2 diffract to 2.5 A
-
crystals of ClpB nucleotide-binding domain diffract to 1.8 A
-
recombinant ClpX lacking the N-terminal Cys cluster domain, i.e. residues 71-446, hanging drop vapor diffusion at 22°C, reservoir solution contains 100 mM imidazole, pH 8.0, 1 M (NH4)2HPO4 and 200 mM NaCl, to obtain crystals of ClpX complexed with nucleotides, 5 mM ADP or ATPgammaS and MgCl2 are added, crystals diffract to 2.6 A
-
41.9-kDa human Hsp70 ATPase domain
-
atomic resolution analysis of the Hsp90 N-terminal domain binding energy landscape by simulating protein dynamics with binding partners such as ATP, ADP, shepherdin. The activity of the molecular chaperone may be linked to local folding-unfolding transitions and conformational switching of the active site lid upon binding and differences in the underlying protein dynamics as a function of the binding partner
-
Bag2-BNB-Hsc70-nucleotide-binding domain complex
-
cDNa sequence encoding alphabeta crystallin inserted into pET16b, expressed in Escherichia coli Bl21
-
crystal structures of four human Hsp70 isoforms are presented: nucleotide binding domains NBDs of HSPA1L, HSPA2, HSPA5 and HSPA6. All four proteins crystallize in a closed cleft conformation, although a slight cleft opening through rotation of subdomain IIB is observed for the HSPA5-ADP complex. The structures presented support the view that the nucleotide binding domains of human Hsp70 function by conserved mechanisms and contribute little to isoform specificity, which instead is brought about by the substrate binding domains and by accessory proteins
-
molecular docking studies with Hsc70 and apoptozole. The 3,5-bis(trifluoromethyl)phenyl group of apoptozole interacts with the binding site of a triphosphate moiety of ATP through polar interactions, and the two 4-methoxy phenyl moieties of apoptozole are located at the adenosine binding site of Hsc70. The CONH2 group of apoptozole can interact with the Glu376 side chain of Hsc70 via a hydrogen-bonding interaction
-
purified recombinant enzyme, X-ray diffraction structure determination and analysis, small angle X-ray scattering, modeling
purified isolated N-terminal domains of ClpB1 bound to GFP, ClpB1-sfGFP, X-ray diffraction structure determination and analysis at 1.8 A resolution
purified isolated N-terminal domains of ClpB1, X-ray diffraction structure determination and analysis at 1.65-2.01 A resolution
crystal structure of yeast Sis1 peptide-binding fragment and Hsp70 Ssa1 C-terminal complex, hanging drop vapour diffusion method, with the mother liquid containing 100 mM Tris/HCl, pH 7.0 and 42.5%(w/v) (NH4)2SO4. The crystals belong to the space group of P4(1)2(1)2 with the cell parameters of a = 112.17 A and c = 171.31 A
-
Hsp90, isoform Hsp82
-
nucleotide-binding domain of Hsp70 in complex with Hsp110 (nucleotide exchange factor Sse1p)
-
44-kDa wild-type stress70c ATPase fragment
-
electron cryomicroscopy reconstruction of ATP-activated trap mutant E271A/E668A, along with native ClpB, in complex with ADP or 5'-adenylyl-beta,gamma-imidodiphosphate, or nucleotide-free. Motif 2 of the ClpB domain M is positioned between the D1-large domains of neighboring subunits and could facilitate a concerted, ATP-driven conformational change in the AAA-1 ring. ATP is essential for high-affinity substrate binding to ClpB and cannot be substituted by 5'-adenylyl-beta,gamma-imidodiphosphate
-
44-kDa wild-type stress70er ATPase fragment
-