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PDBsum entry 1hjo
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protein ligands metals links
Hydrolase PDB id
1hjo

 

 

 

 

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Contents
Protein chain
380 a.a. *
Ligands
ADP
Metals
_CA
_CL
Waters ×199
* Residue conservation analysis
PDB id:
1hjo
Name: Hydrolase
Title: Atpase domain of human heat shock 70kda protein 1
Structure: Protein (heat-shock 70kd protein). Chain: a. Fragment: 42kd atpase n-terminal fragment. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Cellular_location: cytosol. Expressed in: escherichia coli. Expression_system_taxid: 562. Expression_system_cell_line: bl21(de3).
Resolution:
2.30Å     R-factor:   0.203     R-free:   0.253
Authors: J.Osipiuk,M.A.Walsh,B.C.Freeman,R.I.Morimoto,A.Joachimiak
Key ref:
J.Osipiuk et al. (1999). Structure of a new crystal form of human Hsp70 ATPase domain. Acta Crystallogr D Biol Crystallogr, 55, 1105-1107. PubMed id: 10216320 DOI: 10.1107/S0907444999002103
Date:
13-Oct-98     Release date:   21-Oct-98    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P0DMV8  (HS71A_HUMAN) -  Heat shock 70 kDa protein 1A from Homo sapiens
Seq:
Struc: 		 
Seq:
Struc: 		641 a.a.
380 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: E.C.3.6.1.3  - Deleted entry.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: ATP + H2O = ADP + phosphate
ATP
 + H(2)O
 =
ADP
Bound ligand (Het Group name = ADP)
corresponds exactly 		+ phosphate
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    reference    
 
 
DOI no: 10.1107/S0907444999002103 Acta Crystallogr D Biol Crystallogr 55:1105-1107 (1999)
PubMed id: 10216320  
 
 
Structure of a new crystal form of human Hsp70 ATPase domain.
J.Osipiuk, M.A.Walsh, B.C.Freeman, R.I.Morimoto, A.Joachimiak.
 
  ABSTRACT  
 
Hsp70 proteins are highly conserved proteins induced by heat shock and other stress conditions. An ATP-binding domain of human Hsp70 protein has been crystallized in two major morphological forms at pH 7.0 in the presence of PEG 8000 and CaCl2. Both crystal forms belong to the orthorhombic space group P212121, but show no resemblance in unit-cell parameters. Analysis of the crystal structures for both forms shows a 1-2 A shift of one of the subdomains of the protein. This conformational change could reflect a 'natural' flexibility of the protein which might be relevant to ATP binding and may facilitate the interaction of other proteins with Hsp70 protein.
 
  Selected figure(s)  
 
Figure 2.
Figure 2 Least-squares superposition of type I (black) onto type II (cyan) Hsp70 molecules using C^ atoms of the N-terminal domain. Only domain II (residues 189-382) of the protein is shown.
 
  The above figure is reprinted by permission from the IUCr: Acta Crystallogr D Biol Crystallogr (1999, 55, 1105-1107) copyright 1999.  
  Figure was selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
20223214 A.Arakawa, N.Handa, N.Ohsawa, M.Shida, T.Kigawa, F.Hayashi, M.Shirouzu, and S.Yokoyama (2010).
The C-terminal BAG domain of BAG5 induces conformational changes of the Hsp70 nucleotide-binding domain for ADP-ATP exchange.
  Structure, 18, 309-319.
PDB codes: 1ugo 1uk5 2d9d 3a8y
20072699 M.Wisniewska, T.Karlberg, L.Lehtiö, I.Johansson, T.Kotenyova, M.Moche, and H.Schüler (2010).
Crystal structures of the ATPase domains of four human Hsp70 isoforms: HSPA1L/Hsp70-hom, HSPA2/Hsp70-2, HSPA6/Hsp70B', and HSPA5/BiP/GRP78.
  PLoS One, 5, e8625.
PDB codes: 3fe1 3gdq 3i33 3iuc 3jxu
16407317 K.Ruchalski, H.Mao, Z.Li, Z.Wang, S.Gillers, Y.Wang, D.D.Mosser, V.Gabai, J.H.Schwartz, and S.C.Borkan (2006).
Distinct hsp70 domains mediate apoptosis-inducing factor release and nuclear accumulation.
  J Biol Chem, 281, 7873-7880.  
16672609 N.R.Buan, K.Rehfeld, and J.C.Escalante-Semerena (2006).
Studies of the CobA-type ATP:Co(I)rrinoid adenosyltransferase enzyme of Methanosarcina mazei strain Go1.
  J Bacteriol, 188, 3543-3550.  
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.  
15232009 Y.Zhang, and E.R.Zuiderweg (2004).
The 70-kDa heat shock protein chaperone nucleotide-binding domain in solution unveiled as a molecular machine that can reorient its functional subdomains.
  Proc Natl Acad Sci U S A, 101, 10272-10277.  
12724406 W.J.Hung, R.S.Roberson, J.Taft, and D.Y.Wu (2003).
Human BAG-1 proteins bind to the cellular stress response protein GADD34 and interfere with GADD34 functions.
  Mol Cell Biol, 23, 3477-3486.  
12209147 P.Chène (2002).
ATPases as drug targets: learning from their structure.
  Nat Rev Drug Discov, 1, 665-673.  
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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