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
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Research Support, N.I.H., Extramural
MeSH terms
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Amidohydrolases / chemistry*
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Amidohydrolases / genetics
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Amidohydrolases / metabolism
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Amino Acid Sequence
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Carbon Isotopes / chemistry
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Escherichia coli
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Hydrogen / chemistry
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Nitrogen Isotopes / chemistry
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Nuclear Magnetic Resonance, Biomolecular / methods
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Oxazoles / chemistry*
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Oxazoles / metabolism
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Protein Structure, Secondary
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Structural Homology, Protein
Substances
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Carbon Isotopes
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L 161240
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Nitrogen Isotopes
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Oxazoles
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Hydrogen
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Amidohydrolases
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UDP-3-O-acyl-N-acetylglucosamine deacetylase