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http://purl.uniprot.org/citations/15155720http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15155720http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15155720http://www.w3.org/2000/01/rdf-schema#comment"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."xsd:string
http://purl.uniprot.org/citations/15155720http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m402855200"xsd:string
http://purl.uniprot.org/citations/15155720http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m402855200"xsd:string
http://purl.uniprot.org/citations/15155720http://purl.uniprot.org/core/author"Ciszak E.M."xsd:string
http://purl.uniprot.org/citations/15155720http://purl.uniprot.org/core/author"Ciszak E.M."xsd:string
http://purl.uniprot.org/citations/15155720http://purl.uniprot.org/core/author"Honkanen R.E."xsd:string
http://purl.uniprot.org/citations/15155720http://purl.uniprot.org/core/author"Honkanen R.E."xsd:string
http://purl.uniprot.org/citations/15155720http://purl.uniprot.org/core/author"Swingle M.R."xsd:string
http://purl.uniprot.org/citations/15155720http://purl.uniprot.org/core/author"Swingle M.R."xsd:string
http://purl.uniprot.org/citations/15155720http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/15155720http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/15155720http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/15155720http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/15155720http://purl.uniprot.org/core/pages"33992-33999"xsd:string
http://purl.uniprot.org/citations/15155720http://purl.uniprot.org/core/pages"33992-33999"xsd:string
http://purl.uniprot.org/citations/15155720http://purl.uniprot.org/core/title"Structural basis for the catalytic activity of human serine/threonine protein phosphatase-5."xsd:string
http://purl.uniprot.org/citations/15155720http://purl.uniprot.org/core/title"Structural basis for the catalytic activity of human serine/threonine protein phosphatase-5."xsd:string
http://purl.uniprot.org/citations/15155720http://purl.uniprot.org/core/volume"279"xsd:string
http://purl.uniprot.org/citations/15155720http://purl.uniprot.org/core/volume"279"xsd:string
http://purl.uniprot.org/citations/15155720http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/15155720
http://purl.uniprot.org/citations/15155720http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/15155720
http://purl.uniprot.org/citations/15155720http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/15155720
http://purl.uniprot.org/citations/15155720http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/15155720