1s95
Structure of serine/threonine protein phosphatase 5
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OverviewOverview
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.
About this StructureAbout this Structure
1S95 is a Single protein structure of sequence from Homo sapiens with MN, PO4 and MPD as ligands. Active as Phosphoprotein phosphatase, with EC number 3.1.3.16 Full crystallographic information is available from OCA.
ReferenceReference
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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