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

  • Biomol NMR Assign. 2010 Apr;4(1):37-40. doi: 10.1007/s12104-009-9201-5.
Adam W Barb  1 ,  Ling Jiang ,  Christian R H Raetz ,  Pei Zhou
Affiliations
  • 1. Department of Biochemistry, Duke University Medical Center, Durham, NC 27710, USA.
PMID: 19941092 DOI: 10.1007/s12104-009-9201-5
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.

Products