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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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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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Acknowledgments

This research was supported by NIH grants AI-055588 to P. Zhou and GM-51310 to C. R. H. Raetz. A. Barb was supported by the Cellular and Molecular Biology training grant GM-07184 to Duke University.

Conflict of interest statement

The authors declare that they have no conflict of interest.

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Author notes

  1. Adam W. Barb

    Present address: Complex Carbohydrate Research Center, University of Georgia, Athens, GA, 30602, USA

  2. Ling Jiang

    Present address: State Key Laboratory of Magnetic Resonance and Atomic and Molecular Physics, Wuhan Institute of Physics and Mathematics, Chinese Academy of Sciences, Wuhan, 430071, China

Authors and Affiliations

  1. Department of Biochemistry, Duke University Medical Center, Durham, NC, 27710, USA

    Adam W. Barb, Ling Jiang, Christian R. H. Raetz & Pei Zhou

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  1. Adam W. Barb
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  2. Ling Jiang
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  3. Christian R. H. Raetz
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  4. Pei Zhou
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Corresponding author

Correspondence to Pei Zhou.

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Barb, A.W., Jiang, L., Raetz, C.R.H. et al. Assignment of 1H, 13C and 15N backbone resonances of Escherichia coli LpxC bound to L-161,240. Biomol NMR Assign 4, 37–40 (2010). https://doi.org/10.1007/s12104-009-9201-5

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