Assignment of 1H, 13C and 15N backbone resonances of Escherichia coli LpxC bound to L-161,240.
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.
Barb
Adam W
AW
Department of Biochemistry, Duke University Medical Center, Durham, NC 27710, USA.
Jiang
Ling
L
Raetz
Christian R H
CR
Zhou
Pei
P
D000581:Amidohydrolases / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D000595:Amino Acid Sequence; D002247:Carbon Isotopes / Q000737:chemistry; D004926:Escherichia coli; D006859:Hydrogen / Q000737:chemistry; D009587:Nitrogen Isotopes / Q000737:chemistry; D019906:Nuclear Magnetic Resonance, Biomolecular / Q000379:methods; D010080:Oxazoles / Q000737:chemistry* / Q000378:metabolism; D017433:Protein Structure, Secondary; D040681:Structural Homology, Protein
D002247:Carbon Isotopes; C101987:L 161240; D009587:Nitrogen Isotopes; D010080:Oxazoles; D006859:Hydrogen; D000581:Amidohydrolases; C097307:UDP-3-O-acyl-N-acetylglucosamine deacetylase