PDBsum entry 2zbm

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protein metals links
Hydrolase PDB id
Protein chain
331 a.a. *
_ZN ×2
Waters ×449
* Residue conservation analysis
PDB id:
Name: Hydrolase
Title: Crystal structure of i115m mutant cold-active protein tyrosine phosphatase
Structure: Protein-tyrosine-phosphatase. Chain: a. Fragment: residues unp 22-355. Engineered: yes. Mutation: yes
Source: Shewanella sp.. Organism_taxid: 50422. Gene: ppi. Expressed in: escherichia coli. Expression_system_taxid: 562.
1.50Å     R-factor:   0.126     R-free:   0.197
Authors: H.Tsuruta,B.Mikami,C.Yamamoto,H.Yamagata
Key ref: H.Tsuruta et al. (2008). The role of group bulkiness in the catalytic activity of psychrophile cold-active protein tyrosine phosphatase. FEBS J, 275, 4317-4328. PubMed id: 18647345
24-Oct-07     Release date:   29-Jul-08    
Go to PROCHECK summary

Protein chain
Pfam   ArchSchema ?
Q9S427  (Q9S427_9GAMM) -  Protein-tyrosine-phosphatase
361 a.a.
331 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.  - 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     metabolic process   2 terms 
  Biochemical function     hydrolase activity     3 terms  


FEBS J 275:4317-4328 (2008)
PubMed id: 18647345  
The role of group bulkiness in the catalytic activity of psychrophile cold-active protein tyrosine phosphatase.
H.Tsuruta, B.Mikami, C.Yamamoto, H.Yamagata.
The cold-active protein tyrosine phosphatase found in psychrophilic Shewanella species exhibits high catalytic efficiency at low temperatures as well as low thermostability, both of which are characteristics shared by many cold-active enzymes. The structure of cold-active protein tyrosine phosphatase is notable for the presence of three hydrophobic sites (termed the CA, Zn-1 and Zn-2 sites) behind the loop structures comprising the catalytic region. To identify the structural components responsible for specific enzyme characteristics, we determined the structure of wild-type cold-active protein tyrosine phosphatase at high resolution (1.1 A) and measured the catalytic efficiencies of enzymes containing mutations in the three hydrophobic sites. The bulkiness of the amino acid side chains in the core region of the Zn-1 site strongly affects the thermostability and the catalytic efficiency at low temperatures. The mutant enzyme I115M possessed a higher kcat at low temperatures. Elucidation of the crystal structure of I115M at a resolution of 1.5 A revealed that the loop structures involved in retaining the nucleophilic group and the acid catalyst are more flexible than in the wild-type enzyme.

Literature references that cite this PDB file's key reference

  PubMed id Reference
20057143 H.Tsuruta, B.Mikami, T.Higashi, and Y.Aizono (2010).
Crystal structure of cold-active alkaline phosphatase from the psychrophile Shewanella sp.
  Biosci Biotechnol Biochem, 74, 69-74.
PDB code: 3a52
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