| http://purl.uniprot.org/citations/31002736 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/31002736 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/31002736 | http://www.w3.org/2000/01/rdf-schema#comment | "Staphylococcus aureus and other bacterial pathogens affix wall teichoic acids (WTAs) to their surface. These highly abundant anionic glycopolymers have critical functions in bacterial physiology and their susceptibility to β-lactam antibiotics. The membrane-associated TagA glycosyltransferase (GT) catalyzes the first-committed step in WTA biosynthesis and is a founding member of the WecB/TagA/CpsF GT family, more than 6,000 enzymes that synthesize a range of extracellular polysaccharides through a poorly understood mechanism. Crystal structures of TagA from T. italicus in its apo- and UDP-bound states reveal a novel GT fold, and coupled with biochemical and cellular data define the mechanism of catalysis. We propose that enzyme activity is regulated by interactions with the bilayer, which trigger a structural change that facilitates proper active site formation and recognition of the enzyme's lipid-linked substrate. These findings inform upon the molecular basis of WecB/TagA/CpsF activity and could guide the development of new anti-microbial drugs."xsd:string |
| http://purl.uniprot.org/citations/31002736 | http://purl.org/dc/terms/identifier | "doi:10.1371/journal.ppat.1007723"xsd:string |
| http://purl.uniprot.org/citations/31002736 | http://purl.org/dc/terms/identifier | "doi:10.1371/journal.ppat.1007723"xsd:string |
| http://purl.uniprot.org/citations/31002736 | http://purl.uniprot.org/core/author | "Cascio D."xsd:string |
| http://purl.uniprot.org/citations/31002736 | http://purl.uniprot.org/core/author | "Cascio D."xsd:string |
| http://purl.uniprot.org/citations/31002736 | http://purl.uniprot.org/core/author | "Sawaya M.R."xsd:string |
| http://purl.uniprot.org/citations/31002736 | http://purl.uniprot.org/core/author | "Sawaya M.R."xsd:string |
| http://purl.uniprot.org/citations/31002736 | http://purl.uniprot.org/core/author | "Brown E.D."xsd:string |
| http://purl.uniprot.org/citations/31002736 | http://purl.uniprot.org/core/author | "Brown E.D."xsd:string |
| http://purl.uniprot.org/citations/31002736 | http://purl.uniprot.org/core/author | "Kumar G."xsd:string |
| http://purl.uniprot.org/citations/31002736 | http://purl.uniprot.org/core/author | "Kumar G."xsd:string |
| http://purl.uniprot.org/citations/31002736 | http://purl.uniprot.org/core/author | "Clubb R.T."xsd:string |
| http://purl.uniprot.org/citations/31002736 | http://purl.uniprot.org/core/author | "Clubb R.T."xsd:string |
| http://purl.uniprot.org/citations/31002736 | http://purl.uniprot.org/core/author | "Philips M."xsd:string |
| http://purl.uniprot.org/citations/31002736 | http://purl.uniprot.org/core/author | "Philips M."xsd:string |
| http://purl.uniprot.org/citations/31002736 | http://purl.uniprot.org/core/author | "Kattke M.D."xsd:string |
| http://purl.uniprot.org/citations/31002736 | http://purl.uniprot.org/core/author | "Kattke M.D."xsd:string |
| http://purl.uniprot.org/citations/31002736 | http://purl.uniprot.org/core/author | "Gale R.T."xsd:string |
| http://purl.uniprot.org/citations/31002736 | http://purl.uniprot.org/core/author | "Gale R.T."xsd:string |
| http://purl.uniprot.org/citations/31002736 | http://purl.uniprot.org/core/author | "Gosschalk J.E."xsd:string |
| http://purl.uniprot.org/citations/31002736 | http://purl.uniprot.org/core/author | "Gosschalk J.E."xsd:string |
| http://purl.uniprot.org/citations/31002736 | http://purl.uniprot.org/core/author | "Martinez O.E."xsd:string |
| http://purl.uniprot.org/citations/31002736 | http://purl.uniprot.org/core/author | "Martinez O.E."xsd:string |