Structural highlights
Function
[PPP5_HUMAN] May play a role in the regulation of RNA biogenesis and/or mitosis. In vitro, dephosphorylates serine residues of skeletal muscle phosphorylase and histone H1.
Publication Abstract from PubMed
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.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Swingle MR, Honkanen RE, Ciszak EM. Structural basis for the catalytic activity of human serine/threonine protein phosphatase-5. J Biol Chem. 2004 Aug 6;279(32):33992-9. Epub 2004 May 23. PMID:15155720 doi:http://dx.doi.org/10.1074/jbc.M402855200
