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PDBsum entry 1ba1
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protein ligands metals links
Hydrolase PDB id
1ba1

 

 

 

 

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Contents
Protein chain
378 a.a. *
Ligands
ADP
Metals
_MG
_NA
_CL ×2
Waters ×442
* Residue conservation analysis
PDB id:
1ba1
Name: Hydrolase
Title: Heat-shock cognate 70kd protein 44kd atpase n-terminal mutant with cys 17 replaced by lys
Structure: Heat-shock cognate 70kd protein. Chain: a. Fragment: 44kd atpase n-terminal fragment. Engineered: yes. Mutation: yes
Source: Bos taurus. Cattle. Organism_taxid: 9913. Cell_line: bl21 (de3). Organ: brain. Cellular_location: cytosol. Expressed in: escherichia coli. Expression_system_taxid: 562. Expression_system_cell_line: bl21 (de3).
Resolution:
1.70Å     R-factor:   0.202     R-free:   0.244
Authors: S.M.Wilbanks,D.B.Mckay
Key ref:
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. PubMed id: 9585559 DOI: 10.1021/bi973046m
Date:
21-Apr-98     Release date:   15-Jul-98    
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
* PDB and UniProt seqs differ at 1 residue position (black cross)

 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(+)
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    reference    
 
 
DOI no: 10.1021/bi973046m Biochemistry 37:7456-7462 (1998)
PubMed id: 9585559  
 
 
Structural replacement of active site monovalent cations by the epsilon-amino group of lysine in the ATPase fragment of bovine Hsc70.
S.M.Wilbanks, D.B.McKay.
 
  ABSTRACT  
 
We have assessed the ability of the epsilon-amino group of a non-native lysine chain to substitute for a monovalent cation in an enzyme active site. In the bovine Hsc70 ATPase fragment, mutation of cysteine 17 or aspartic acid 206 to lysine potentially allows the replacement of an active site potassium ion with the epsilon-amino nitrogen. We examined the ATP hydrolysis kinetics and crystal structures of isolated mutant ATPase domains. The introduced epsilon-amino nitrogen in the C17K mutant occupies a significantly different position than the potassium ion. The introduced epsilon-amino nitrogen in the D206K mutant occupies a position indistinguishable from that of the potassium in the wild-type structure. Each mutant retains <5% ATPase activity when compared to the wild type under physiological conditions (potassium buffer) although substrate binding is tighter, probably as a consequence of slower release. It is possible to construct a very good structural mimic of bound cation which suffices for substrate binding but not for catalytic activity.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
18329094 E.Di Cera (2008).
Thrombin.
  Mol Aspects Med, 29, 203-254.  
17428793 F.Marino, Z.W.Chen, C.E.Ergenekan, L.A.Bush-Pelc, F.S.Mathews, and E.Di Cera (2007).
Structural basis of Na+ activation mimicry in murine thrombin.
  J Biol Chem, 282, 16355-16361.
PDB codes: 2ocv 2od3
17996706 J.Jiang, E.G.Maes, A.B.Taylor, L.Wang, A.P.Hinck, E.M.Lafer, and R.Sousa (2007).
Structural basis of J cochaperone binding and regulation of Hsp70.
  Mol Cell, 28, 422-433.
PDB codes: 2qw9 2qwl 2qwm 2qwn 2qwo 2qwp 2qwq 2qwr
17426134 J.Y.Ha, H.K.Kim, d.o. .J.Kim, K.H.Kim, S.J.Oh, H.H.Lee, H.J.Yoon, H.K.Song, and S.W.Suh (2007).
The recombination-associated protein RdgC adopts a novel toroidal architecture for DNA binding.
  Nucleic Acids Res, 35, 2671-2681.
PDB code: 2owy
16905543 J.Oria-Hernández, H.Riveros-Rosas, and L.Ramírez-Sílva (2006).
Dichotomic phylogenetic tree of the pyruvate kinase family: K+ -dependent and -independent enzymes.
  J Biol Chem, 281, 30717-30724.  
16855243 K.Yang, Y.Eyobo, L.A.Brand, D.Martynowski, D.Tomchick, E.Strauss, and H.Zhang (2006).
Crystal structure of a type III pantothenate kinase: insight into the mechanism of an essential coenzyme A biosynthetic enzyme universally distributed in bacteria.
  J Bacteriol, 188, 5532-5540.
PDB code: 2gtd
16428384 L.A.Bush, R.W.Nelson, and E.Di Cera (2006).
Murine thrombin lacks Na+ activation but retains high catalytic activity.
  J Biol Chem, 281, 7183-7188.  
16455491 M.Vogel, B.Bukau, and M.P.Mayer (2006).
Allosteric regulation of Hsp70 chaperones by a proline switch.
  Mol Cell, 21, 359-367.  
15537659 Y.Wu, X.Qian, Y.He, I.A.Moya, and Y.Luo (2005).
Crystal structure of an ATPase-active form of Rad51 homolog from Methanococcus voltae. Insights into potassium dependence.
  J Biol Chem, 280, 722-728.
PDB code: 1xu4
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.  
11288181 D.B.Roy, T.Rose, and E.Di Cera (2001).
Replacement of thrombin residue G184 with Lys or Arg fails to mimic Na+ binding.
  Proteins, 43, 315-318.  
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
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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