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http://purl.uniprot.org/citations/11163217http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11163217http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/11163217http://www.w3.org/2000/01/rdf-schema#comment"Salmonella spp. utilize a specialized protein secretion system to deliver a battery of effector proteins into host cells. Several of these effectors stimulate Cdc42- and Rac1-dependent cytoskeletal changes that promote bacterial internalization. These potentially cytotoxic alterations are rapidly reversed by the effector SptP, a tyrosine phosphatase and GTPase activating protein (GAP) that targets Cdc42 and Rac1. The 2.3 A resolution crystal structure of an SptP-Rac1 transition state complex reveals an unusual GAP architecture that mimics host functional homologs. The phosphatase domain possesses a conserved active site but distinct surface properties. Binding to Rac1 induces a dramatic stabilization in SptP of a four-helix bundle that makes extensive contacts with the Switch I and Switch II regions of the GTPase."xsd:string
http://purl.uniprot.org/citations/11163217http://purl.org/dc/terms/identifier"doi:10.1016/s1097-2765(00)00141-6"xsd:string
http://purl.uniprot.org/citations/11163217http://purl.org/dc/terms/identifier"doi:10.1016/s1097-2765(00)00141-6"xsd:string
http://purl.uniprot.org/citations/11163217http://purl.uniprot.org/core/author"Galan J.E."xsd:string
http://purl.uniprot.org/citations/11163217http://purl.uniprot.org/core/author"Galan J.E."xsd:string
http://purl.uniprot.org/citations/11163217http://purl.uniprot.org/core/author"Stebbins C.E."xsd:string
http://purl.uniprot.org/citations/11163217http://purl.uniprot.org/core/author"Stebbins C.E."xsd:string
http://purl.uniprot.org/citations/11163217http://purl.uniprot.org/core/date"2000"xsd:gYear
http://purl.uniprot.org/citations/11163217http://purl.uniprot.org/core/date"2000"xsd:gYear
http://purl.uniprot.org/citations/11163217http://purl.uniprot.org/core/name"Mol. Cell"xsd:string
http://purl.uniprot.org/citations/11163217http://purl.uniprot.org/core/name"Mol. Cell"xsd:string
http://purl.uniprot.org/citations/11163217http://purl.uniprot.org/core/pages"1449-1460"xsd:string
http://purl.uniprot.org/citations/11163217http://purl.uniprot.org/core/pages"1449-1460"xsd:string
http://purl.uniprot.org/citations/11163217http://purl.uniprot.org/core/title"Modulation of host signaling by a bacterial mimic: structure of the Salmonella effector SptP bound to Rac1."xsd:string
http://purl.uniprot.org/citations/11163217http://purl.uniprot.org/core/title"Modulation of host signaling by a bacterial mimic: structure of the Salmonella effector SptP bound to Rac1."xsd:string
http://purl.uniprot.org/citations/11163217http://purl.uniprot.org/core/volume"6"xsd:string
http://purl.uniprot.org/citations/11163217http://purl.uniprot.org/core/volume"6"xsd:string
http://purl.uniprot.org/citations/11163217http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/11163217
http://purl.uniprot.org/citations/11163217http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/11163217
http://purl.uniprot.org/citations/11163217http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/11163217
http://purl.uniprot.org/citations/11163217http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/11163217
http://purl.uniprot.org/uniprot/P74873http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/11163217
http://purl.uniprot.org/uniprot/P63000http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/11163217