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http://purl.uniprot.org/citations/21300288http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/21300288http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/21300288http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Citation
http://purl.uniprot.org/citations/21300288http://www.w3.org/2000/01/rdf-schema#comment"The virulence of Gram-positive bacteria is enhanced by toxins like the Streptococcus pyogenes β-NAD(+) glycohydrolase known as SPN. SPN-producing strains of S. pyogenes additionally express the protein immunity factor for SPN (IFS), which forms an inhibitory complex with SPN. We have determined crystal structures of the SPN-IFS complex and IFS alone, revealing that SPN is structurally related to ADP-ribosyl transferases but lacks the canonical binding site for protein substrates. SPN is instead a highly efficient glycohydrolase with the potential to deplete cellular levels of β-NAD(+). The protective effect of IFS involves an extensive interaction with the SPN active site that blocks access to β-NAD(+). The conformation of IFS changes upon binding to SPN, with repacking of an extended C-terminal α helix into a compact shape. IFS is an attractive target for the development of novel bacteriocidal compounds functioning by blocking the bacterium's self-immunity to the SPN toxin."xsd:string
http://purl.uniprot.org/citations/21300288http://purl.org/dc/terms/identifier"doi:10.1016/j.str.2010.12.013"xsd:string
http://purl.uniprot.org/citations/21300288http://purl.org/dc/terms/identifier"doi:10.1016/j.str.2010.12.013"xsd:string
http://purl.uniprot.org/citations/21300288http://purl.uniprot.org/core/author"Ellenberger T."xsd:string
http://purl.uniprot.org/citations/21300288http://purl.uniprot.org/core/author"Ellenberger T."xsd:string
http://purl.uniprot.org/citations/21300288http://purl.uniprot.org/core/author"Hultgren S.J."xsd:string
http://purl.uniprot.org/citations/21300288http://purl.uniprot.org/core/author"Hultgren S.J."xsd:string
http://purl.uniprot.org/citations/21300288http://purl.uniprot.org/core/author"Smith C.L."xsd:string
http://purl.uniprot.org/citations/21300288http://purl.uniprot.org/core/author"Smith C.L."xsd:string
http://purl.uniprot.org/citations/21300288http://purl.uniprot.org/core/author"Pinkner J.S."xsd:string
http://purl.uniprot.org/citations/21300288http://purl.uniprot.org/core/author"Pinkner J.S."xsd:string
http://purl.uniprot.org/citations/21300288http://purl.uniprot.org/core/author"Caparon M.G."xsd:string
http://purl.uniprot.org/citations/21300288http://purl.uniprot.org/core/author"Caparon M.G."xsd:string
http://purl.uniprot.org/citations/21300288http://purl.uniprot.org/core/author"Elam J.S."xsd:string
http://purl.uniprot.org/citations/21300288http://purl.uniprot.org/core/author"Elam J.S."xsd:string
http://purl.uniprot.org/citations/21300288http://purl.uniprot.org/core/author"Ghosh J."xsd:string
http://purl.uniprot.org/citations/21300288http://purl.uniprot.org/core/author"Ghosh J."xsd:string
http://purl.uniprot.org/citations/21300288http://purl.uniprot.org/core/date"2011"xsd:gYear
http://purl.uniprot.org/citations/21300288http://purl.uniprot.org/core/date"2011"xsd:gYear
http://purl.uniprot.org/citations/21300288http://purl.uniprot.org/core/name"Structure"xsd:string
http://purl.uniprot.org/citations/21300288http://purl.uniprot.org/core/name"Structure"xsd:string
http://purl.uniprot.org/citations/21300288http://purl.uniprot.org/core/pages"192-202"xsd:string