PDBsum entry 2gi4

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protein links
Hydrolase PDB id
Protein chain
156 a.a. *
* Residue conservation analysis
PDB id:
Name: Hydrolase
Title: Solution structure of the low molecular weight protein tyrosine phosphatase from campylobacter jejuni.
Structure: Possible phosphotyrosine protein phosphatase. Chain: a. Engineered: yes
Source: Campylobacter jejuni. Organism_taxid: 197. Strain: 11168. Gene: cj1258. Expressed in: escherichia coli. Expression_system_taxid: 562.
NMR struc: 10 models
Authors: D.Tolkatchev,R.Shaykhutdinov,P.Xu,F.Ni
Key ref: D.Tolkatchev et al. (2006). Three-dimensional structure and ligand interactions of the low molecular weight protein tyrosine phosphatase from Campylobacter jejuni. Protein Sci, 15, 2381-2394. PubMed id: 17008719 DOI: 10.1110/ps.062279806
28-Mar-06     Release date:   18-Apr-06    
Go to PROCHECK summary

Protein chain
Pfam   ArchSchema ?
Q0P8Z8  (Q0P8Z8_CAMJE) -  Putative phosphotyrosine protein phosphatase
151 a.a.
156 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 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     peptidyl-tyrosine dephosphorylation   2 terms 
  Biochemical function     hydrolase activity     2 terms  


DOI no: 10.1110/ps.062279806 Protein Sci 15:2381-2394 (2006)
PubMed id: 17008719  
Three-dimensional structure and ligand interactions of the low molecular weight protein tyrosine phosphatase from Campylobacter jejuni.
D.Tolkatchev, R.Shaykhutdinov, P.Xu, J.Plamondon, D.C.Watson, N.M.Young, F.Ni.
A putative low molecular weight protein tyrosine phosphatase (LMW-PTP) was identified in the genome sequence of the bacterial pathogen, Campylobacter jejuni. This novel gene, cj1258, has sequence homology with a distinctive class of phosphatases widely distributed among prokaryotes and eukaryotes. We report here the solution structure of Cj1258 established by high-resolution NMR spectroscopy using NOE-derived distance restraints, hydrogen bond data, and torsion angle restraints. The three-dimensional structure consists of a central four-stranded parallel beta-sheet flanked by five alpha-helices, revealing an overall structural topology similar to those of the eukaryotic LMW-PTPs, such as human HCPTP-A, bovine BPTP, and Saccharomyces cerevisiae LTP1, and to those of the bacterial LMW-PTPs MPtpA from Mycobacterium tuberculosis and YwlE from Bacillus subtilis. The active site of the enzyme is flexible in solution and readily adapts to the binding of ligands, such as the phosphate ion. An NMR-based screen was carried out against a number of potential inhibitors and activators, including phosphonomethylphenylalanine, derivatives of the cinnamic acid, 2-hydroxy-5-nitrobenzaldehyde, cinnamaldehyde, adenine, and hypoxanthine. Despite its bacterial origin, both the three-dimensional structure and ligand-binding properties of Cj1258 suggest that this novel phosphatase may have functional roles close to those of eukaryotic and mammalian tyrosine phosphatases. The three-dimensional structure along with mapping of small-molecule binding will be discussed in the context of developing high-affinity inhibitors of this novel LMW-PTP.

Literature references that cite this PDB file's key reference

  PubMed id Reference
18240386 C.E.Hubbard, and A.M.Barrios (2008).
A highly efficient route to enantiomerically pure l-N-Bz-Pmp(t-Bu)2-OH and incorporation into a peptide-based protein tyrosine phosphatase inhibitor.
  Bioorg Med Chem Lett, 18, 679-681.  
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