Crystal structure of lipid A disaccharide synthase LpxB from Escherichia coli
Abstract
Most Gram-negative bacteria are surrounded by a glycolipid called lipopolysaccharide (LPS), which forms a barrier to hydrophobic toxins and, in pathogenic bacteria, is a virulence factor. During LPS biosynthesis, a membrane-associated glycosyltransferase (LpxB) forms a tetra-acylated disaccharide that is further acylated to form the membrane anchor moiety of LPS. Here we solve the structure of a soluble and catalytically competent LpxB by X-ray crystallography. The structure reveals that LpxB has a glycosyltransferase-B family fold but with a highly intertwined, C-terminally swapped dimer comprising four domains. We identify key catalytic residues with a product, UDP, bound in the active site, as well as clusters of hydrophobic residues that likely mediate productive membrane association or capture of lipidic substrates. These studies provide the basis for rational design of antibiotics targeting a crucial step in LPS biosynthesis.
- Authors:
-
[1];
- Univ. of Minnesota Twin Cities, Minneapolis, MN (United States)
- Univ. of Minnesota Twin Cities, Minneapolis, MN (United States); Bristol-Myers Squibb, Redwood City, CA (United States)
- Publication Date:
- Research Org.:
- Argonne National Laboratory (ANL), Argonne, IL (United States)
- Sponsoring Org.:
- USDOE Office of Science (SC), Basic Energy Sciences (BES). Scientific User Facilities Division; National Inst. of Health; NIH-ORIP HEI
- OSTI Identifier:
- 1431361
- Grant/Contract Number:
- AC02-06CH11357; P41 GM103403; S10 RR029205; GM118047
- Resource Type:
- Accepted Manuscript
- Journal Name:
- Nature Communications
- Additional Journal Information:
- Journal Volume: 9; Journal Issue: 1; Journal ID: ISSN 2041-1723
- Publisher:
- Nature Publishing Group
- Country of Publication:
- United States
- Language:
- ENGLISH
- Subject:
- 59 BASIC BIOLOGICAL SCIENCES; Bacterial structural biology; Enzymes; X-ray crystallography
Citation Formats
Bohl, Thomas E., Shi, Ke, Lee, John K., and Aihara, Hideki. Crystal structure of lipid A disaccharide synthase LpxB from Escherichia coli. United States: N. p., 2018.
Web. doi:10.1038/s41467-017-02712-9.
Bohl, Thomas E., Shi, Ke, Lee, John K., & Aihara, Hideki. Crystal structure of lipid A disaccharide synthase LpxB from Escherichia coli. United States. https://doi.org/10.1038/s41467-017-02712-9
Bohl, Thomas E., Shi, Ke, Lee, John K., and Aihara, Hideki. Thu .
"Crystal structure of lipid A disaccharide synthase LpxB from Escherichia coli". United States. https://doi.org/10.1038/s41467-017-02712-9. https://www.osti.gov/servlets/purl/1431361.
@article{osti_1431361,
title = {Crystal structure of lipid A disaccharide synthase LpxB from Escherichia coli},
author = {Bohl, Thomas E. and Shi, Ke and Lee, John K. and Aihara, Hideki},
abstractNote = {Most Gram-negative bacteria are surrounded by a glycolipid called lipopolysaccharide (LPS), which forms a barrier to hydrophobic toxins and, in pathogenic bacteria, is a virulence factor. During LPS biosynthesis, a membrane-associated glycosyltransferase (LpxB) forms a tetra-acylated disaccharide that is further acylated to form the membrane anchor moiety of LPS. Here we solve the structure of a soluble and catalytically competent LpxB by X-ray crystallography. The structure reveals that LpxB has a glycosyltransferase-B family fold but with a highly intertwined, C-terminally swapped dimer comprising four domains. We identify key catalytic residues with a product, UDP, bound in the active site, as well as clusters of hydrophobic residues that likely mediate productive membrane association or capture of lipidic substrates. These studies provide the basis for rational design of antibiotics targeting a crucial step in LPS biosynthesis.},
doi = {10.1038/s41467-017-02712-9},
journal = {Nature Communications},
number = 1,
volume = 9,
place = {United States},
year = {Thu Jan 25 00:00:00 EST 2018},
month = {Thu Jan 25 00:00:00 EST 2018}
}
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