| http://purl.uniprot.org/citations/25023290 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/25023290 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Citation |
| http://purl.uniprot.org/citations/25023290 | http://www.w3.org/2000/01/rdf-schema#comment | "The membrane-bound tetraacyldisaccharide-1-phosphate 4'-kinase, LpxK, catalyzes the sixth step of the lipid A (Raetz) biosynthetic pathway and is a viable antibiotic target against emerging Gram-negative pathogens. We report the crystal structure of lipid IVA, the LpxK product, bound to the enzyme, providing a rare glimpse into interfacial catalysis and the surface scanning strategy by which many poorly understood lipid modification enzymes operate. Unlike the few previously structurally characterized proteins that bind lipid A or its precursors, LpxK binds almost exclusively to the glucosamine/phosphate moieties of the lipid molecule. Steady-state kinetic analysis of multiple point mutants of the lipid-binding pocket pinpoints critical residues involved in substrate binding, and characterization of N-terminal helix truncation mutants uncovers the role of this substructure as a hydrophobic membrane anchor. These studies make critical contributions to the limited knowledge surrounding membrane-bound enzymes that act upon lipid substrates and provide a structural template for designing small molecule inhibitors targeting this essential kinase."xsd:string |
| http://purl.uniprot.org/citations/25023290 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m114.589986"xsd:string |
| http://purl.uniprot.org/citations/25023290 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.m114.589986"xsd:string |
| http://purl.uniprot.org/citations/25023290 | http://purl.uniprot.org/core/author | "Zhou P."xsd:string |
| http://purl.uniprot.org/citations/25023290 | http://purl.uniprot.org/core/author | "Schumacher M.A."xsd:string |
| http://purl.uniprot.org/citations/25023290 | http://purl.uniprot.org/core/author | "York J.D."xsd:string |
| http://purl.uniprot.org/citations/25023290 | http://purl.uniprot.org/core/author | "Tonthat N.K."xsd:string |
| http://purl.uniprot.org/citations/25023290 | http://purl.uniprot.org/core/author | "Emptage R.P."xsd:string |
| http://purl.uniprot.org/citations/25023290 | http://purl.uniprot.org/core/date | "2014"xsd:gYear |
| http://purl.uniprot.org/citations/25023290 | http://purl.uniprot.org/core/name | "J Biol Chem"xsd:string |
| http://purl.uniprot.org/citations/25023290 | http://purl.uniprot.org/core/pages | "24059-24068"xsd:string |
| http://purl.uniprot.org/citations/25023290 | http://purl.uniprot.org/core/title | "Structural basis of lipid binding for the membrane-embedded tetraacyldisaccharide-1-phosphate 4'-kinase LpxK."xsd:string |
| http://purl.uniprot.org/citations/25023290 | http://purl.uniprot.org/core/volume | "289"xsd:string |
| http://purl.uniprot.org/citations/25023290 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/25023290 |
| http://purl.uniprot.org/citations/25023290 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/25023290 |
| http://purl.uniprot.org/citations/25023290 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/25023290 |
| http://purl.uniprot.org/citations/25023290 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/25023290 |
| http://purl.uniprot.org/enzyme/2.7.1.130 | http://purl.uniprot.org/core/citation | http://purl.uniprot.org/citations/25023290 |
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| http://purl.uniprot.org/uniprot/O67572 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/25023290 |