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1xxp

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[[Image:1xxp.gif|left|200px]]
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{{STRUCTURE_1xxp| PDB=1xxp | SCENE= }}
{{STRUCTURE_1xxp| PDB=1xxp | SCENE= }}
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'''Yersinia YopH (residues 163-468) C403S binds phosphotyrosyl peptide at two sites'''
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===Yersinia YopH (residues 163-468) C403S binds phosphotyrosyl peptide at two sites===
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==Overview==
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YopH is a protein tyrosine phosphatase and an essential virulence determinant of the pathogenic bacterium Yersinia. Yersinia delivers YopH into infected host cells using a type III secretion mechanism. YopH dephosphorylates several focal adhesion proteins including p130Cas in human epithelial cells, resulting in disruption of focal adhesions and cell detachment from the extracellular matrix. How the C-terminal protein tyrosine phosphatase domain of YopH targets specific substrates such as p130Cas in the complex milieu of the host cell has not been fully elucidated. An N-terminal non-catalytic domain of YopH binds p130Cas in a phosphotyrosine-dependent manner and functions as a novel substrate-targeting site. The structure of the YopH protein tyrosine phosphatase domain bound to a model phosphopeptide substrate was solved and the resulting structure revealed a second substrate-targeting site ('site 2') within the catalytic domain. Site 2 binds to p130Cas in a phosphotyrosine-dependent manner, and co-operates with the N-terminal domain ('site 1') to promote efficient recognition of p130Cas by YopH in epithelial cells. The identification of two substrate-targeting sites in YopH that co-operate to promote epithelial cell detachment and bacterial virulence reinforces the importance of protein-protein interactions for determining protein tyrosine phosphatase specificity in vivo, and highlights the sophisticated nature of microbial pathogenicity factors.
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{{ABSTRACT_PUBMED_15720545}}
==About this Structure==
==About this Structure==
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[[Category: Stuckey, J A.]]
[[Category: Stuckey, J A.]]
[[Category: Peptide binds at site remote from catalytic site. important for protein localization in infected cell.]]
[[Category: Peptide binds at site remote from catalytic site. important for protein localization in infected cell.]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 15:38:21 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 15:10:27 2008''

Revision as of 12:10, 29 July 2008

Image:1xxp.png

Template:STRUCTURE 1xxp

Yersinia YopH (residues 163-468) C403S binds phosphotyrosyl peptide at two sites

Template:ABSTRACT PUBMED 15720545

About this Structure

1XXP is a Single protein structure of sequence from Yersinia enterocolitica. Full crystallographic information is available from OCA.

Reference

Two substrate-targeting sites in the Yersinia protein tyrosine phosphatase co-operate to promote bacterial virulence., Ivanov MI, Stuckey JA, Schubert HL, Saper MA, Bliska JB, Mol Microbiol. 2005 Mar;55(5):1346-56. PMID:15720545

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