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. Epub 2009 Nov 26.

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.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Amidohydrolases / chemistry*
  • Amidohydrolases / genetics
  • Amidohydrolases / metabolism
  • Amino Acid Sequence
  • Carbon Isotopes / chemistry
  • Escherichia coli
  • Hydrogen / chemistry
  • Nitrogen Isotopes / chemistry
  • Nuclear Magnetic Resonance, Biomolecular / methods
  • Oxazoles / chemistry*
  • Oxazoles / metabolism
  • Protein Structure, Secondary
  • Structural Homology, Protein

Substances

  • Carbon Isotopes
  • L 161240
  • Nitrogen Isotopes
  • Oxazoles
  • Hydrogen
  • Amidohydrolases
  • UDP-3-O-acyl-N-acetylglucosamine deacetylase