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http://purl.uniprot.org/citations/24446487http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/24446487http://www.w3.org/2000/01/rdf-schema#comment"Pathogenic bacteria introduce effector proteins directly into the cytosol of eukaryotic cells to promote invasion and colonization. OspG, a Shigella spp. effector kinase, plays a role in this process by helping to suppress the host inflammatory response. OspG has been reported to bind host E2 ubiquitin-conjugating enzymes activated with ubiquitin (E2~Ub), a key enzyme complex in ubiquitin transfer pathways. A co-crystal structure of the OspG/UbcH5c~Ub complex reveals that complex formation has important ramifications for the activity of both OspG and the UbcH5c~Ub conjugate. OspG is a minimal kinase domain containing only essential elements required for catalysis. UbcH5c~Ub binding stabilizes an active conformation of the kinase, greatly enhancing OspG kinase activity. In contrast, interaction with OspG stabilizes an extended, less reactive form of UbcH5c~Ub. Recognizing conserved E2 features, OspG can interact with at least ten distinct human E2s~Ub. Mouse oral infection studies indicate that E2~Ub conjugates act as novel regulators of OspG effector kinase function in eukaryotic host cells."xsd:string
http://purl.uniprot.org/citations/24446487http://purl.org/dc/terms/identifier"doi:10.1002/embj.201386386"xsd:string
http://purl.uniprot.org/citations/24446487http://purl.uniprot.org/core/author"Swaney D.L."xsd:string
http://purl.uniprot.org/citations/24446487http://purl.uniprot.org/core/author"Scott J.D."xsd:string
http://purl.uniprot.org/citations/24446487http://purl.uniprot.org/core/author"Villen J."xsd:string
http://purl.uniprot.org/citations/24446487http://purl.uniprot.org/core/author"Le Trong I."xsd:string
http://purl.uniprot.org/citations/24446487http://purl.uniprot.org/core/author"Stadnyk A.W."xsd:string
http://purl.uniprot.org/citations/24446487http://purl.uniprot.org/core/author"Stenkamp R.E."xsd:string
http://purl.uniprot.org/citations/24446487http://purl.uniprot.org/core/author"Klevit R.E."xsd:string
http://purl.uniprot.org/citations/24446487http://purl.uniprot.org/core/author"Smith F.D."xsd:string
http://purl.uniprot.org/citations/24446487http://purl.uniprot.org/core/author"Pruneda J.N."xsd:string
http://purl.uniprot.org/citations/24446487http://purl.uniprot.org/core/author"Brzovic P.S."xsd:string
http://purl.uniprot.org/citations/24446487http://purl.uniprot.org/core/author"Rohde J.R."xsd:string
http://purl.uniprot.org/citations/24446487http://purl.uniprot.org/core/author"Daurie A."xsd:string
http://purl.uniprot.org/citations/24446487http://purl.uniprot.org/core/date"2014"xsd:gYear
http://purl.uniprot.org/citations/24446487http://purl.uniprot.org/core/name"EMBO J"xsd:string
http://purl.uniprot.org/citations/24446487http://purl.uniprot.org/core/pages"437-449"xsd:string
http://purl.uniprot.org/citations/24446487http://purl.uniprot.org/core/title"E2~Ub conjugates regulate the kinase activity of Shigella effector OspG during pathogenesis."xsd:string
http://purl.uniprot.org/citations/24446487http://purl.uniprot.org/core/volume"33"xsd:string
http://purl.uniprot.org/citations/24446487http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/24446487
http://purl.uniprot.org/citations/24446487http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/24446487
http://purl.uniprot.org/uniprot/#_A8K674-mappedCitation-24446487http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/24446487
http://purl.uniprot.org/uniprot/#_D6RAH7-mappedCitation-24446487http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/24446487
http://purl.uniprot.org/uniprot/#_P0CG48-mappedCitation-24446487http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/24446487