PDBsum entry: 2z72

Hydrolase

PDB id: 2z72

Contents

Protein chain

338 a.a. *

Metals

_ZN ×2

Waters ×772

* Residue conservation analysis

PDB id:

2z72

Name:

Hydrolase

Title:

New structure of cold-active protein tyrosine phosphatase at 1.1 angstrom

Structure:

Protein-tyrosine-phosphatase. Chain: a. Fragment: unp residues 22-361. Synonym: cold-active protein tyrosine phosphtase. Engineered: yes

Source:

Shewanella sp.. Organism_taxid: 50422. Gene: ppi. Expressed in: escherichia coli. Expression_system_taxid: 562.

Resolution:

1.10Å R-factor: 0.110 R-free: 0.161

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 DOI: 10.1111/j.1742-4658.2008.06575.x

Date:

10-Aug-07 Release date: 29-Jul-08

Protein chain

Q9S427  (Q9S427_9GAMM) -  Protein-tyrosine-phosphatase

Seq: 361 a.a.

Struc: 338 a.a.*

* PDB and UniProt seqs differ at 1 residue position (black cross)

Enzyme reactions

• Enzyme class: E.C.3.1.3.48 - Protein-tyrosine-phosphatase.
• Reaction: Protein tyrosine phosphate + H₂O = protein tyrosine + phosphate

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

 Gene Ontology (GO) functional annotation 

• Biochemical function: hydrolase activity (2 terms)

reference

DOI no: 10.1111/j.1742-4658.2008.06575.x

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.

ABSTRACT

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 k(cat) 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.