ArticleNature communications2018
Crystal structure of lipid A disaccharide synthase LpxB from Escherichia coli.
Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 25 citations in OpenAlex.
- Rational Design of Natural Xanthones Against Gram-negative Bacteria.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Chemical strategies for antisense antibiotics.Chemical Society reviews · 2024Review
- Enhancing effect of natural adjuvant, panduratin A, on antibacterial activity of colistin against multidrug-resistant Acinetobacter baumannii.Scientific reports · 2024Article
- Metagenomic insights into the composition and function of the gut microbiota of mice infected withFrontiers in immunology · 2023Article
- Microbial Proteins in Stomach Biopsies Associated with Gastritis, Ulcer, and Gastric Cancer.Molecules (Basel, Switzerland) · 2022Article
- Article
- Comparative Transcriptomic Analyses of Haemophilus parasuis Reveal Differently Expressed Genes among Strains with Different Virulence Degrees.Current microbiology · 2021Article
- Genomic and Transcriptomic Analysis of BovineFrontiers in veterinary science · 2021Article
- Pharmacoinformatics approaches to identify potential hits against tetraacyldisaccharide 4'-kinase (LpxK) ofRSC advances · 2020Article
- Changes of the human skin microbiota upon chronic exposure to polycyclic aromatic hydrocarbon pollutants.Microbiome · 2020Article
- MnmE, a Central tRNA-Modifying GTPase, Is Essential for the Growth, Pathogenicity, and Arginine Metabolism ofFrontiers in cellular and infection microbiology · 2019Article
- The substrate-binding cap of the UDP-diacylglucosamine pyrophosphatase LpxH is highly flexible, enabling facile substrate binding and product release.The Journal of biological chemistry · 2018Article
- Current Progress in the Structural and Biochemical Characterization of Proteins Involved in the Assembly of Lipopolysaccharide.International journal of microbiology · 2018Review
Corrections and comments
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Authors and funding
4 authors at 1 institution in 2 countries.
Funding
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.
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