Assignment of 1H, 13C and 15N backbone resonances of Escherichia coli LpxC bound to L-161,240.
Publication
, Journal Article
Barb, AW; Jiang, L; Raetz, CRH; Zhou, P
Published in: Biomol NMR Assign
April 2010
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.
Duke Scholars
Published In
Biomol NMR Assign
DOI
EISSN
1874-270X
Publication Date
April 2010
Volume
4
Issue
1
Start / End Page
37 / 40
Location
Netherlands
Related Subject Headings
- Structural Homology, Protein
- Protein Structure, Secondary
- Oxazoles
- Nuclear Magnetic Resonance, Biomolecular
- Nitrogen Isotopes
- Hydrogen
- Escherichia coli
- Carbon Isotopes
- Biophysics
- Amino Acid Sequence
Citation
APA
Chicago
ICMJE
MLA
NLM
Barb, A. W., Jiang, L., Raetz, C. R. H., & Zhou, P. (2010). Assignment of 1H, 13C and 15N backbone resonances of Escherichia coli LpxC bound to L-161,240. Biomol NMR Assign, 4(1), 37–40. https://doi.org/10.1007/s12104-009-9201-5
Barb, Adam W., Ling Jiang, Christian R. H. Raetz, and Pei Zhou. “Assignment of 1H, 13C and 15N backbone resonances of Escherichia coli LpxC bound to L-161,240.” Biomol NMR Assign 4, no. 1 (April 2010): 37–40. https://doi.org/10.1007/s12104-009-9201-5.
Barb AW, Jiang L, Raetz CRH, Zhou P. 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.
Barb, Adam W., et al. “Assignment of 1H, 13C and 15N backbone resonances of Escherichia coli LpxC bound to L-161,240.” Biomol NMR Assign, vol. 4, no. 1, Apr. 2010, pp. 37–40. Pubmed, doi:10.1007/s12104-009-9201-5.
Barb AW, Jiang L, Raetz CRH, Zhou P. 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.
Published In
Biomol NMR Assign
DOI
EISSN
1874-270X
Publication Date
April 2010
Volume
4
Issue
1
Start / End Page
37 / 40
Location
Netherlands
Related Subject Headings
- Structural Homology, Protein
- Protein Structure, Secondary
- Oxazoles
- Nuclear Magnetic Resonance, Biomolecular
- Nitrogen Isotopes
- Hydrogen
- Escherichia coli
- Carbon Isotopes
- Biophysics
- Amino Acid Sequence