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PDBsum entry 3qy8

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protein ligands metals links
Hydrolase PDB id
3qy8
Jmol
Contents
Protein chain
243 a.a.
Ligands
SO4
GOL ×2
Metals
_FE ×2
_MG
Waters ×240
PDB id:
3qy8
Name: Hydrolase
Title: Crystal structures of ywqe from bacillus subtilis and cpsb f streptococcus pneumoniae, unique metal-dependent tyrosine phosphatases
Structure: Tyrosine-protein phosphatase cpsb. Chain: a. Engineered: yes
Source: Streptococcus pneumoniae. Organism_taxid: 1313. Gene: cpsb, sp_0347, wzh. Expressed in: escherichia coli. Expression_system_taxid: 562.
Resolution:
2.00Å     R-factor:   0.183     R-free:   0.233
Authors: H.S.Kim,S.J.Lee,H.J.Yoon,D.R.An,D.J.Kim,S.-J.Kim,S.W.Suh
Key ref: H.S.Kim et al. (2011). Crystal structures of YwqE from Bacillus subtilis and CpsB from Streptococcus pneumoniae, unique metal-dependent tyrosine phosphatases. J Struct Biol, 175, 442-450. PubMed id: 21605684 DOI: 10.1016/j.jsb.2011.05.007
Date:
03-Mar-11     Release date:   08-Jun-11    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q9AHD4  (CPSB1_STRPN) -  Tyrosine-protein phosphatase CpsB
Seq:
Struc:
243 a.a.
243 a.a.
Key:    PfamA domain  Secondary structure

 Enzyme reactions 
   Enzyme class: E.C.3.1.3.48  - Protein-tyrosine-phosphatase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: Protein tyrosine phosphate + H2O = protein tyrosine + phosphate
Protein tyrosine phosphate
+ H(2)O
= protein tyrosine
+ phosphate
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Biological process     peptidyl-tyrosine dephosphorylation   4 terms 
  Biochemical function     catalytic activity     5 terms  

 

 
    reference    
 
 
DOI no: 10.1016/j.jsb.2011.05.007 J Struct Biol 175:442-450 (2011)
PubMed id: 21605684  
 
 
Crystal structures of YwqE from Bacillus subtilis and CpsB from Streptococcus pneumoniae, unique metal-dependent tyrosine phosphatases.
H.S.Kim, S.J.Lee, H.J.Yoon, D.R.An, d.o. .J.Kim, S.J.Kim, S.W.Suh.
 
  ABSTRACT  
 
Unique metal-dependent protein tyrosine phosphatases that belong to the polymerase and histindinol phosphatase (PHP) family are present in Gram-positive bacteria. They are distinct from the Cys-based, low-molecular-weight phosphotyrosine protein phosphatases (LMPTPs). Two representative members of the PHP family tyrosine phosphatases are YwqE from Bacillus subtilis and CpsB from Streptococcus pneumoniae. YwqE is involved in polysaccharide biosynthesis, bacterial DNA metabolism, and DNA damage response in B. subtilis. CpsB regulates capsular polysaccharide biosynthesis via tyrosine dephosphorylation of CpsD, its cognate tyrosine kinase, in S. pneumoniae. To gain insights into the active site and possible conformational changes of the metal-dependent tyrosine phosphatases from Gram-positive bacteria, we have determined the crystal structures of B. subtilis YwqE (in both the apo form and the phosphate-bound form) and S. pneumoniae CpsB (in the sulfate-bound form). Comparisons of the three structures reveal conformational plasticity of two active site loops. Furthermore, in both structures of the phosphate-bound YwqE and the sulfate-bound CpsB, the phosphate (or sulfate) ion is bound to a cluster of three metal ions in the active site, thus providing insight into the pre-catalytic state.