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http://purl.uniprot.org/citations/9702193http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9702193http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/9702193http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Citation
http://purl.uniprot.org/citations/9702193http://www.w3.org/2000/01/rdf-schema#comment"VanX is a zinc-dependent D-alanyl-D-alanine dipeptidase that is a critical component in a system that mediates transposon-based vancomycin resistance in enterococci. It is also a key drug target in circumventing clinical vancomycin resistance. The structure of VanX from E. faecium has been solved by X-ray crystallography and reveals a Zn(2+)-dipeptidase with a unique overall fold and a well-defined active site confined within a cavity of limited size. The crystal structures of VanX, the VanX:D-alanyl-D-alanine complex, the VanX:D-alanine complex, and VanX in complex with phosphonate and phosphinate transition-state analog inhibitors, are also presented at high resolution. Structural homology searches of known structures revealed that the fold of VanX is similar to those of two proteins: the N-terminal fragment of murine Sonic hedgehog and the Zn(2+)-dependent N-acyl-D-alanyl-D-alanine carboxypeptidase of S. albus G."xsd:string
http://purl.uniprot.org/citations/9702193http://purl.org/dc/terms/identifier"doi:10.1016/s1097-2765(00)80115-x"xsd:string
http://purl.uniprot.org/citations/9702193http://purl.org/dc/terms/identifier"doi:10.1016/s1097-2765(00)80115-x"xsd:string
http://purl.uniprot.org/citations/9702193http://purl.uniprot.org/core/author"Park C.H."xsd:string
http://purl.uniprot.org/citations/9702193http://purl.uniprot.org/core/author"Park C.H."xsd:string
http://purl.uniprot.org/citations/9702193http://purl.uniprot.org/core/author"Katz L."xsd:string
http://purl.uniprot.org/citations/9702193http://purl.uniprot.org/core/author"Katz L."xsd:string
http://purl.uniprot.org/citations/9702193http://purl.uniprot.org/core/author"Bussiere D.E."xsd:string
http://purl.uniprot.org/citations/9702193http://purl.uniprot.org/core/author"Bussiere D.E."xsd:string
http://purl.uniprot.org/citations/9702193http://purl.uniprot.org/core/author"Pratt S.D."xsd:string
http://purl.uniprot.org/citations/9702193http://purl.uniprot.org/core/author"Pratt S.D."xsd:string
http://purl.uniprot.org/citations/9702193http://purl.uniprot.org/core/author"Severin J.M."xsd:string
http://purl.uniprot.org/citations/9702193http://purl.uniprot.org/core/author"Severin J.M."xsd:string
http://purl.uniprot.org/citations/9702193http://purl.uniprot.org/core/author"Holzman T."xsd:string
http://purl.uniprot.org/citations/9702193http://purl.uniprot.org/core/author"Holzman T."xsd:string
http://purl.uniprot.org/citations/9702193http://purl.uniprot.org/core/date"1998"xsd:gYear
http://purl.uniprot.org/citations/9702193http://purl.uniprot.org/core/date"1998"xsd:gYear
http://purl.uniprot.org/citations/9702193http://purl.uniprot.org/core/name"Mol. Cell"xsd:string
http://purl.uniprot.org/citations/9702193http://purl.uniprot.org/core/name"Mol. Cell"xsd:string
http://purl.uniprot.org/citations/9702193http://purl.uniprot.org/core/pages"75-84"xsd:string
http://purl.uniprot.org/citations/9702193http://purl.uniprot.org/core/pages"75-84"xsd:string
http://purl.uniprot.org/citations/9702193http://purl.uniprot.org/core/title"The structure of VanX reveals a novel amino-dipeptidase involved in mediating transposon-based vancomycin resistance."xsd:string