1S95

Structure of serine/threonine protein phosphatase 5

Summary for 1S95

• Entry DOI: 10.2210/pdb1s95/pdb
• Descriptor: Serine/threonine protein phosphatase 5, MANGANESE (II) ION, PHOSPHATE ION, ... (5 entities in total)
• Functional Keywords: protein phosphatase, pppase, pp5, phosphate anion, metal ion, metallophosphoesterase, hydrolase
• Biological source: Homo sapiens (human)
• Cellular location: Nucleus : P53041
• Total number of polymer chains: 2
• Total formula weight: 76420.08

Authors

Swingle, M.R.,Honkanen, R.E.,Ciszak, E.M. (deposition date: 2004-02-03, release date: 2004-08-24, Last modification date: 2023-08-23)

Primary citation

Swingle, M.R.,Honkanen, R.E.,Ciszak, E.M.
Structural basis for the catalytic activity of human serine/threonine protein phosphatase-5.
J.Biol.Chem., 279:33992-33999, 2004

PubMed Abstract: 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.

PubMed: 15155720
DOI: 10.1074/jbc.M402855200

Experimental method

X-RAY DIFFRACTION (1.6 Å)