ArticleProceedings of the National Academy of Sciences of the United States of America2012
Structural and mechanistic analysis of the membrane-embedded glycosyltransferase WaaA required for lipopolysaccharide synthesis.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 47 citations in OpenAlex.
- Structure and function of Salmonella inner membrane.Archives of microbiology · 2026Review
- Klebsiella pneumoniae O-polysaccharide biosynthesis highlights the diverse organization of catalytic modules in ABC transporter-dependent glycan assembly.The Journal of biological chemistry · 2024Article
- Cryo-EM analysis ofScience advances · 2024Article
- Article
- Crystal structure of the lipopolysaccharide outer core galactosyltransferase WaaB involved in pathogenic bacterial invasion of host cells.Frontiers in microbiology · 2023Article
- Interplays of mutations inFrontiers in cellular and infection microbiology · 2023Article
- The Role of the Gut Microbiome in Diabetes and Obesity-Related Kidney Disease.International journal of molecular sciences · 2021Review
- The surprising structural and mechanistic dichotomy of membrane-associated phosphoglycosyl transferases.Biochemical Society transactions · 2021Review
- Conserved Conformational Hierarchy across Functionally Divergent Glycosyltransferases of the GT-B Structural Superfamily as Determined from Microsecond Molecular Dynamics.International journal of molecular sciences · 2021Article
- Expression, purification, and characterization of a new Glucosyltransferase involved in the third step of O-antigen repeating-unit biosynthesis of Escherichia coli O152.Glycoconjugate journal · 2020Article
- Structural and mechanistic themes in glycoconjugate biosynthesis at membrane interfaces.Current opinion in structural biology · 2019Review
- Monotopic Membrane Proteins Join the Fold.Trends in biochemical sciences · 2019Review
- Crystal structure of lipid A disaccharide synthase LpxB from Escherichia coli.Nature communications · 2018Article
- Current Progress in the Structural and Biochemical Characterization of Proteins Involved in the Assembly of Lipopolysaccharide.International journal of microbiology · 2018Review
- Elucidating endotoxin-biomolecule interactions with FRET: extending the frontiers of their supramolecular complexation.Journal of biological methods · 2017Review
- Biochemical Characterization of Bifunctional 3-Deoxy-β-d-manno-oct-2-ulosonic Acid (β-Kdo) Transferase KpsC from Escherichia coli Involved in Capsule Biosynthesis.The Journal of biological chemistry · 2016Article
- Enzymatic synthesis of 3-deoxy-d-manno-octulosonic acid (KDO) and its application for LPS assembly.Bioorganic & medicinal chemistry letters · 2016Article
- Genetic and Molecular Basis of Kingella kingae Encapsulation.Infection and immunity · 2016Article
- Bacterial β-Kdo glycosyltransferases represent a new glycosyltransferase family (GT99).Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Kdo2 -lipid A: structural diversity and impact on immunopharmacology.Biological reviews of the Cambridge Philosophical Society · 2015Review
Corrections and comments
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Authors and funding
11 authors at 4 institutions in 4 countries.
Funding
Abstract
WaaA is a key enzyme in the biosynthesis of LPS, a critical component of the outer envelope of Gram-negative bacteria. Embedded in the cytoplasmic face of the inner membrane, WaaA catalyzes the transfer of 3-deoxy-d-manno-oct-2-ulosonic acid (Kdo) to the lipid A precursor of LPS. Here we present crystal structures of the free and CMP-bound forms of WaaA from Aquifex aeolicus, an ancient Gram-negative hyperthermophile. These structures reveal details of the CMP-binding site and implicate a unique sequence motif (GGS/TX(5)GXNXLE) in Kdo binding. In addition, a cluster of highly conserved amino acid residues was identified which represents the potential membrane-attachment and acceptor-substrate binding site of WaaA. A series of site-directed mutagenesis experiments revealed critical roles for glycine 30 and glutamate 31 in Kdo transfer. Our results provide the structural basis of a critical reaction in LPS biosynthesis and allowed the development of a detailed model of the catalytic mechanism of WaaA.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.