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Structural Basis for the Catalytic Activity of Human Serine/Threonine Protein Phosphatase-5Serinehhreonine 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 resolved the mechanism for PP5-mediated hydrolysis of phosphoprotein substrates, which requires the precise positioning of two metal ions within a con served Aspn-271-M(sub 1):M(sub 2)-W(sup 1)-His-427-His-304-Asp-274 catalytic motif. The structure of PPSc 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.
Document ID
20040047245
Acquisition Source
Marshall Space Flight Center
Document Type
Preprint (Draft being sent to journal)
Authors
Swingle, M. R.
(NASA Marshall Space Flight Center Huntsville, AL, United States)
Honkanen, R.
(NASA Marshall Space Flight Center Huntsville, AL, United States)
Ciszak, E. M.
(NASA Marshall Space Flight Center Huntsville, AL, United States)
Date Acquired
August 21, 2013
Publication Date
January 1, 2004
Subject Category
Life Sciences (General)
Distribution Limits
Public
Copyright
Work of the US Gov. Public Use Permitted.

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