| Literature DB >> 19941092 |
Adam W Barb1, Ling Jiang, Christian R H Raetz, Pei Zhou.
Abstract
The UDP-3-O-(R-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase LpxC catalyzes the committed reaction of lipid A biosynthesis, an essential pathway in Gram-negative bacteria. We report the backbone resonance assignments of the 34 kDa LpxC from Escherichia coli in complex with the antibiotic L-161,240 using multidimensional, multinuclear NMR experiments. The (1)H chemical shifts of complexed L-161,240 are also determined.Entities:
Mesh:
Substances:
Year: 2009 PMID: 19941092 PMCID: PMC3631426 DOI: 10.1007/s12104-009-9201-5
Source DB: PubMed Journal: Biomol NMR Assign ISSN: 1874-270X Impact factor: 0.746