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Assignment of 1H, 13C and 15N backbone resonances of Escherichia coli LpxC bound to L-161,240 |
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| Authors: | Adam W. Barb Ling Jiang Christian R. H. Raetz Pei Zhou |
| Affiliation: | 1. Department of Biochemistry, Duke University Medical Center, Durham, NC, 27710, USA 2. Complex Carbohydrate Research Center, University of Georgia, Athens, GA, 30602, USA 3. State Key Laboratory of Magnetic Resonance and Atomic and Molecular Physics, Wuhan Institute of Physics and Mathematics, Chinese Academy of Sciences, Wuhan, 430071, China |
| 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 1H chemical shifts of complexed L-161,240 are also determined. |
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