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Search The CSA
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Catalytic Site Atlas

CSA LITERATURE entry for 1ytw

E.C. nameprotein-tyrosine-phosphatase
SpeciesYersinia enterocolitica (Bacteria)
E.C. Number (IntEnz) 3.1.3.48
CSA Homologues of 1ytwThere are 67 Homologs
CSA Entries With UniProtID P15273
CSA Entries With EC Number 3.1.3.48
PDBe Entry 1ytw
PDBSum Entry 1ytw
MACiE Entry M0047

Literature Report

Introduction The protein tyrosine phosphatases are a group of enzymes that remove the phosphate groups from tyrosine residues. These enzymes are important in cell signalling during growth and development and act antagonistically with the protein tyrosine kinases.
The PTP family is subdivided into several groups including the tyrosine specific receptor and non-receptor-like enzymes, the dual-specificity group, the low molecular weight PTPs and the cdc25 group. All members share the same mechanism of hydrolysis and are characterised by a CX5R sequence motif. However the cdc25 group is highly divergent. A cysteine-phosphate intermediate is formed during the reaction and is then hydrolysed. Although the different groups of PTPs are relatively divergent their active sites are highly conserved.
Mechansim The CX5R motif forms a loop that provides an oxyanion hole for the stabilisation of the phosphate group. Binding to this loop causes the movement of a conserved aspartic acid into the active site. The reaction proceeds in two steps: cys acts as a nucleophile and becomes covalently bound to the phosphate group. The PO3 is then transferred to a water molecule. The arg residue is important for the geometric orientation of the PO3.
Reaction

Catalytic Sites for 1ytw

Annotated By Reference To The Literature - Site 1 (Perform Site Search)
ResidueChainNumberUniProtKB NumberFunctional PartFunctionTargetDescription
AspA356356macie:sideChain
ThrA410410macie:sideChain
CysA403403macie:sideChain
ArgA409409macie:sideChain
GluA290290macie:sideChain
HisA402402macie:sideChain

Literature References

Notes:
Fauman EB
The X-ray crystal structures of Yersinia tyrosine phosphatase with bound tungstate and nitrate. Mechanistic implications.
J Biol Chem 1996 271 18780-18788
PubMed: 8702535
Wang F
Conformational and dynamic changes of Yersinia protein tyrosine phosphatase induced by ligand binding and active site mutation and revealed by H/D exchange and electrospray ionization Fourier transform ion cyclotron resonance mass spectrometry.
Biochemistry 1998 37 15289-15299
PubMed: 9799489
Fauman EB
Structure and function of the protein tyrosine phosphatases.
Trends Biochem Sci 1996 21 413-417
PubMed: 8987394
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