1s95: Difference between revisions

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[[Image:1s95.gif|left|200px]]
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{{STRUCTURE_1s95|  PDB=1s95  |  SCENE=  }}  
{{STRUCTURE_1s95|  PDB=1s95  |  SCENE=  }}  


'''Structure of serine/threonine protein phosphatase 5'''
===Structure of serine/threonine protein phosphatase 5===




==Overview==
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Serine/threonine protein phosphatase-5 (PP5) affects many signaling networks that regulate cell growth and cellular responses to stress. Here we report the crystal structure of the PP5 catalytic domain (PP5c) at a resolution of 1.6 A. From this structure we propose a mechanism for PP5-mediated hydrolysis of phosphoprotein substrates, which requires the precise positioning of two metal ions within a conserved Asp271-M1:M2-W1-His427-His304-Asp274 catalytic motif (where M1 and M2 are metals and W1 is a water molecule). The structure of PP5c provides a structural basis for explaining the exceptional catalytic proficiency of protein phosphatases, which are among the most powerful known catalysts. Resolution of the entire C terminus revealed a novel subdomain, and the structure of the PP5c should also aid development of type-specific inhibitors.
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{{ABSTRACT_PUBMED_15155720}}


==About this Structure==
==About this Structure==
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[[Category: Pppase]]
[[Category: Pppase]]
[[Category: Protein phosphatase]]
[[Category: Protein phosphatase]]
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Revision as of 11:54, 28 July 2008

File:1s95.png

Template:STRUCTURE 1s95

Structure of serine/threonine protein phosphatase 5

Template:ABSTRACT PUBMED 15155720

About this Structure

1S95 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Structural basis for the catalytic activity of human serine/threonine protein phosphatase-5., Swingle MR, Honkanen RE, Ciszak EM, J Biol Chem. 2004 Aug 6;279(32):33992-9. Epub 2004 May 23. PMID:15155720

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