| http://purl.uniprot.org/citations/17698807 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/17698807 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/17698807 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Citation |
| http://purl.uniprot.org/citations/17698807 | http://www.w3.org/2000/01/rdf-schema#comment | "UDP-N-acetylglucosamine (UDP-GlcNAc) acyltransferase (LpxA) catalyzes the first step of lipid A biosynthesis, the reversible transfer of the R-3-hydroxyacyl chain from R-3-hydroxyacyl acyl carrier protein to the glucosamine 3-OH group of UDP-GlcNAc. Escherichia coli LpxA is highly selective for R-3-hydroxymyristate. The crystal structure of the E. coli LpxA homotrimer, determined previously in the absence of lipid substrates or products, revealed that LpxA contains an unusual, left-handed parallel beta-helix fold. We have now solved the crystal structures of E. coli LpxA with the bound product UDP-3-O-(R-3-hydroxymyristoyl)-GlcNAc at a resolution of 1.74 A and with bound UDP-3-O-(R-3-hydroxydecanoyl)-GlcNAc at 1.85 A. The structures of these complexes are consistent with the catalytic mechanism deduced by mutagenesis and with a recent 3.0-A structure of LpxA with bound UDP-GlcNAc. Our structures show how LpxA selects for 14-carbon R-3-hydroxyacyl chains and reveal two modes of UDP binding."xsd:string |
| http://purl.uniprot.org/citations/17698807 | http://purl.org/dc/terms/identifier | "doi:10.1073/pnas.0705833104"xsd:string |
| http://purl.uniprot.org/citations/17698807 | http://purl.org/dc/terms/identifier | "doi:10.1073/pnas.0705833104"xsd:string |
| http://purl.uniprot.org/citations/17698807 | http://purl.org/dc/terms/identifier | "doi:10.1073/pnas.0705833104"xsd:string |
| http://purl.uniprot.org/citations/17698807 | http://purl.uniprot.org/core/author | "Raetz C.R."xsd:string |
| http://purl.uniprot.org/citations/17698807 | http://purl.uniprot.org/core/author | "Raetz C.R."xsd:string |
| http://purl.uniprot.org/citations/17698807 | http://purl.uniprot.org/core/author | "Williams A.H."xsd:string |
| http://purl.uniprot.org/citations/17698807 | http://purl.uniprot.org/core/author | "Williams A.H."xsd:string |
| http://purl.uniprot.org/citations/17698807 | http://purl.uniprot.org/core/date | "2007"xsd:gYear |
| http://purl.uniprot.org/citations/17698807 | http://purl.uniprot.org/core/date | "2007"xsd:gYear |
| http://purl.uniprot.org/citations/17698807 | http://purl.uniprot.org/core/name | "Proc. Natl. Acad. Sci. U.S.A."xsd:string |
| http://purl.uniprot.org/citations/17698807 | http://purl.uniprot.org/core/name | "Proc. Natl. Acad. Sci. U.S.A."xsd:string |
| http://purl.uniprot.org/citations/17698807 | http://purl.uniprot.org/core/pages | "13543-13550"xsd:string |
| http://purl.uniprot.org/citations/17698807 | http://purl.uniprot.org/core/pages | "13543-13550"xsd:string |
| http://purl.uniprot.org/citations/17698807 | http://purl.uniprot.org/core/title | "Structural basis for the acyl chain selectivity and mechanism of UDP-N-acetylglucosamine acyltransferase."xsd:string |
| http://purl.uniprot.org/citations/17698807 | http://purl.uniprot.org/core/title | "Structural basis for the acyl chain selectivity and mechanism of UDP-N-acetylglucosamine acyltransferase."xsd:string |
| http://purl.uniprot.org/citations/17698807 | http://purl.uniprot.org/core/volume | "104"xsd:string |
| http://purl.uniprot.org/citations/17698807 | http://purl.uniprot.org/core/volume | "104"xsd:string |
| http://purl.uniprot.org/citations/17698807 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/17698807 |
| http://purl.uniprot.org/citations/17698807 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/17698807 |
| http://purl.uniprot.org/citations/17698807 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/17698807 |
| http://purl.uniprot.org/citations/17698807 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/17698807 |