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PDBsum entry 1hpm
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Hydrolase (acting on acid anhydrides) PDB id
1hpm

 

 

 

 

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Contents
Protein chain
378 a.a. *
Ligands
PO4
ADP
Metals
_MG
__K ×2
_CL ×2
Waters ×429
* Residue conservation analysis
PDB id:
1hpm
Name: Hydrolase (acting on acid anhydrides)
Title: How potassium affects the activity of the molecular chaperone hsc70. Ii. Potassium binds specifically in the atpase active site
Structure: 44k atpase fragment (n-terminal) of 7o kd heat-shock cognate protein. Chain: a. Engineered: yes
Source: Bos taurus. Cattle. Organism_taxid: 9913. Organ: brain. Expressed in: escherichia coli. Expression_system_taxid: 562
Resolution:
1.70Å     R-factor:   0.205    
Authors: S.M.Wilbanks,D.B.Mckay
Key ref: S.M.Wilbanks and D.B.McKay (1995). How potassium affects the activity of the molecular chaperone Hsc70. II. Potassium binds specifically in the ATPase active site. J Biol Chem, 270, 2251-2257. PubMed id: 7836458
Date:
24-Mar-95     Release date:   31-Jul-95    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P19120  (HSP7C_BOVIN) -  Heat shock cognate 71 kDa protein from Bos taurus
Seq:
Struc: 		 
Seq:
Struc: 		650 a.a.
378 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.3.6.4.10  - non-chaperonin molecular chaperone ATPase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: ATP + H2O = ADP + phosphate + H+
ATP
 + H2O
 =
ADP
Bound ligand (Het Group name = ADP)
corresponds exactly 		+ phosphate
 + H(+)
Bound ligand (Het Group name = PO4)
corresponds exactly
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    reference    
 
 
J Biol Chem 270:2251-2257 (1995)
PubMed id: 7836458  
 
 
How potassium affects the activity of the molecular chaperone Hsc70. II. Potassium binds specifically in the ATPase active site.
S.M.Wilbanks, D.B.McKay.
 
  ABSTRACT  
 
Crystallographic anomalous scattering from potassium at 1.7 A resolution reveals two monovalent ions that interact with MgADP and P(i) in the nucleotide binding cleft of wild-type recombinant bovine Hsc70 ATPase fragment. K+ at site 1 interacts with oxygens of the beta-phosphate of ADP, whereas K+ at site 2 interacts with an oxygen of P(i). Both K+ ions also interact with specific H2O molecules in the first hydration shell of the octahedrally coordinated Mg2+ ion and with specific protein ligands. In crystals that have Na+ present, K+ is replaced by a Na+ ion at site 1 and by a Na(+)-H2O pair at site 2. The K+ ions are positioned where they could stabilize binding of a beta,gamma-bidentate MgATP complex with Hsc70, as well as a transition state during ATP hydrolysis, suggesting that monovalent ions act as specific metal cofactors in the ATPase reaction of Hsc70.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
20018538 A.Bhattacharya, M.Revington, and E.R.Zuiderweg (2010).
Measurement and interpretation of 15N-1H residual dipolar couplings in larger proteins.
  J Magn Reson, 203, 11-28.  
  19908379 Y.Liu, and I.Bahar (2010).
Toward understanding allosteric signaling mechanisms in the ATPase domain of molecular chaperones.
  Pac Symp Biocomput, (), 269-280.  
  20862304 Y.Liu, L.M.Gierasch, and I.Bahar (2010).
Role of Hsp70 ATPase domain intrinsic dynamics and sequence evolution in enabling its functional interactions with NEFs.
  PLoS Comput Biol, 6, 0.  
19883127 H.J.Woo, J.Jiang, E.M.Lafer, and R.Sousa (2009).
ATP-induced conformational changes in Hsp70: molecular dynamics and experimental validation of an in silico predicted conformation.
  Biochemistry, 48, 11470-11477.  
19694756 J.Cellitti, Z.Zhang, S.Wang, B.Wu, H.Yuan, P.Hasegawa, D.G.Guiney, and M.Pellecchia (2009).
Small molecule DnaK modulators targeting the beta-domain.
  Chem Biol Drug Des, 74, 349-357.  
18329094 E.Di Cera (2008).
Thrombin.
  Mol Aspects Med, 29, 203-254.  
18495488 R.E.Joseph, and A.H.Andreotti (2008).
Bacterial expression and purification of interleukin-2 tyrosine kinase: single step separation of the chaperonin impurity.
  Protein Expr Purif, 60, 194-197.  
18555782 S.Polier, Z.Dragovic, F.U.Hartl, and A.Bracher (2008).
Structural basis for the cooperation of Hsp70 and Hsp110 chaperones in protein folding.
  Cell, 133, 1068-1079.
PDB codes: 3d2e 3d2f
18954053 S.Varma, and S.B.Rempe (2008).
Structural transitions in ion coordination driven by changes in competition for ligand binding.
  J Am Chem Soc, 130, 15405-15419.  
17499050 B.J.Nolen, and T.D.Pollard (2007).
Insights into the influence of nucleotides on actin family proteins from seven structures of Arp2/3 complex.
  Mol Cell, 26, 449-457.
PDB codes: 2p9i 2p9k 2p9l 2p9n 2p9p 2p9s 2p9u
16763562 A.Scrima, and A.Wittinghofer (2006).
Dimerisation-dependent GTPase reaction of MnmE: how potassium acts as GTPase-activating element.
  EMBO J, 25, 2940-2951.
PDB codes: 2gj8 2gj9 2gja
16905099 B.S.Hong, M.K.Yun, Y.M.Zhang, S.Chohnan, C.O.Rock, S.W.White, S.Jackowski, H.W.Park, and R.Leonardi (2006).
Prokaryotic type II and type III pantothenate kinases: The same monomer fold creates dimers with distinct catalytic properties.
  Structure, 14, 1251-1261.
PDB codes: 2ews 2f9t 2f9w
17131193 S.Takeuchi (2006).
Molecular cloning, sequence, function and structural basis of human heart 150 kDa oxygen-regulated protein, an ER chaperone.
  Protein J, 25, 517-528.  
15947196 C.M.Manlandro, D.H.Haydon, and A.G.Rosenwald (2005).
Ability of Sit4p to promote K+ efflux via Nha1p is modulated by Sap155p and Sap185p.
  Eukaryot Cell, 4, 1041-1049.  
15273304 J.M.Gruschus, L.E.Greene, E.Eisenberg, and J.A.Ferretti (2004).
Experimentally biased model structure of the Hsc70/auxilin complex: substrate transfer and interdomain structural change.
  Protein Sci, 13, 2029-2044.  
14612565 S.Prasad, K.J.Wright, D.Banerjee Roy, L.A.Bush, A.M.Cantwell, and E.Di Cera (2003).
Redesigning the monovalent cation specificity of an enzyme.
  Proc Natl Acad Sci U S A, 100, 13785-13790.  
11532005 A.Padiglia, R.Medda, A.Lorrai, M.Paci, J.Z.Pedersen, A.Boffi, A.Bellelli, A.F.Agrò, and G.Floris (2001).
Irreversible inhibition of pig kidney copper-containing amine oxidase by sodium and lithium ions.
  Eur J Biochem, 268, 4686-4697.  
11536359 O.Schueler-Furman, Y.Altuvia, and H.Margalit (2001).
Examination of possible structural constraints of MHC-binding peptides by assessment of their native structure within their source proteins.
  Proteins, 45, 47-54.  
11248194 T.H.Wilson, and P.Z.Ding (2001).
Sodium-substrate cotransport in bacteria.
  Biochim Biophys Acta, 1505, 121-130.  
10841532 S.L.De Wall, E.S.Meadows, L.J.Barbour, and G.W.Gokel (2000).
Synthetic receptors as models for alkali metal cation-pi binding sites in proteins.
  Proc Natl Acad Sci U S A, 97, 6271-6276.  
10077555 D.A.Debe, M.J.Carlson, and W.A.Goddard (1999).
The topomer-sampling model of protein folding.
  Proc Natl Acad Sci U S A, 96, 2596-2601.  
10491176 H.Schüler, E.Korenbaum, C.E.Schutt, U.Lindberg, and R.Karlsson (1999).
Mutational analysis of Ser14 and Asp157 in the nucleotide-binding site of beta-actin.
  Eur J Biochem, 265, 210-220.  
9799500 M.C.Sousa, and D.B.McKay (1998).
The hydroxyl of threonine 13 of the bovine 70-kDa heat shock cognate protein is essential for transducing the ATP-induced conformational change.
  Biochemistry, 37, 15392-15399.
PDB codes: 1bup 2bup
9585559 S.M.Wilbanks, and D.B.McKay (1998).
Structural replacement of active site monovalent cations by the epsilon-amino group of lysine in the ATPase fragment of bovine Hsc70.
  Biochemistry, 37, 7456-7462.
PDB codes: 1ba0 1ba1
9753476 W.J.Chirico, M.L.Markey, and A.L.Fink (1998).
Conformational changes of an Hsp70 molecular chaperone induced by nucleotides, polypeptides, and N-ethylmaleimide.
  Biochemistry, 37, 13862-13870.  
9083109 M.Sriram, J.Osipiuk, B.Freeman, R.Morimoto, and A.Joachimiak (1997).
Human Hsp70 molecular chaperone binds two calcium ions within the ATPase domain.
  Structure, 5, 403-414.
PDB code: 1s3x
9145101 S.Rüdiger, A.Buchberger, and B.Bukau (1997).
Interaction of Hsp70 chaperones with substrates.
  Nat Struct Biol, 4, 342-349.  
9251782 W.Wriggers, and K.Schulten (1997).
Stability and dynamics of G-actin: back-door water diffusion and behavior of a subdomain 3/4 loop.
  Biophys J, 73, 624-639.  
8620890 B.Feifel, E.Sandmeier, H.J.Schönfeld, and P.Christen (1996).
Potassium ions and the molecular-chaperone activity of DnaK.
  Eur J Biochem, 237, 318-321.  
8688415 E.R.Guinto, and E.Di Cera (1996).
Large heat capacity change in a protein-monovalent cation interaction.
  Biochemistry, 35, 8800-8804.  
  8918457 H.C.Schneider, B.Westermann, W.Neupert, and M.Brunner (1996).
The nucleotide exchange factor MGE exerts a key function in the ATP-dependent cycle of mt-Hsp70-Tim44 interaction driving mitochondrial protein import.
  EMBO J, 15, 5796-5803.  
8608143 R.Zhang, V.Villeret, W.N.Lipscomb, and H.J.Fromm (1996).
Kinetics and mechanisms of activation and inhibition of porcine liver fructose-1,6-bisphosphatase by monovalent cations.
  Biochemistry, 35, 3038-3043.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB codes are shown on the right.

 

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