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Assignment of 1H, 13C and 15N backbone resonances of Escherichia coli LpxC bound to L-161,240.

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.

SUBMITTER: Barb AW

PROVIDER: S-EPMC3631426 | biostudies-literature | 2010 Apr

REPOSITORIES: biostudies-literature

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Assignment of 1H, 13C and 15N backbone resonances of Escherichia coli LpxC bound to L-161,240.

Barb Adam W AW Jiang Ling L Raetz Christian R H CR Zhou Pei P

Biomolecular NMR assignments 20091126 1

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. ...[more]

PMID: 19941092

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