ArticleProceedings of the National Academy of Sciences of the United States of America2007
Structural basis for the acyl chain selectivity and mechanism of UDP-N-acetylglucosamine acyltransferase.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
43 citing papers in PubMed, 82 citations in OpenAlex.
- Differential membrane lipid disruption by lipopeptide antibiotics, colistin and turnercyclamycins.Nature communications · 2026Article
- Decoding a Gut Commensal Signal: Structural and Immunological Profiling of Segatella Copri Lipopolysaccharide.Angewandte Chemie (International ed. in English) · 2025Article
- Review on Current Research on Biosynthesis of Biosurfactants and the Regulation Influenced by Metal Ions.Journal of microbiology and biotechnology · 2025Review
- The fatty acid synthesis geneMicrobiology spectrum · 2025Article
- Reliable Chemical Synthesis of UDP-3-Organic letters · 2024Article
- The role of the essential GTPase ObgE in regulating lipopolysaccharide synthesis in Escherichia coli.Nature communications · 2024Article
- Signaling through theJournal of bacteriology · 2024Article
- Lipid-Centric Approaches in Combating Infectious Diseases: Antibacterials, Antifungals and Antivirals with Lipid-Associated Mechanisms of Action.Antibiotics (Basel, Switzerland) · 2023Review
- Antibacterial activities of anthraquinones: structure-activity relationships and action mechanisms.RSC medicinal chemistry · 2023Review
- LipidA-IDER to Explore the Global Lipid A Repertoire of Drug-Resistant Gram-Negative Bacteria.Analytical chemistry · 2023Article
- Identification and prioritization of potential therapeutic molecules against LpxA fromCurrent research in structural biology · 2023Article
- Glycoconjugates: Synthesis, Functional Studies, and Therapeutic Developments.Chemical reviews · 2022Review
- Ecogenomics reveals viral communities across the Challenger Deep oceanic trench.Communications biology · 2022Article
- Uncovering lipopolysaccharide regulation in bacteria via the critical lipid binding tunnel of YciS/YciM.iScience · 2022Article
- Extraction and bioinformatics analysis of Chlamydia trachomatis LpxA.International ophthalmology · 2021Article
- Structure-Based Virtual Screening ofBiomolecules · 2020Article
- Discovery of dual-activity small-molecule ligands of Pseudomonas aeruginosa LpxA and LpxD using SPR and X-ray crystallography.Scientific reports · 2019Article
- Structure guided design of an antibacterial peptide that targets UDP-N-acetylglucosamine acyltransferase.Scientific reports · 2019Article
- Network-Based Metabolism-Centered Screening of Potential Drug Targets inFrontiers in cellular and infection microbiology · 2019Article
- Crystal structure of lipid A disaccharide synthase LpxB from Escherichia coli.Nature communications · 2018Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
UDP-N-acetylglucosamine (UDP-GlcNAc) acyltransferase (LpxA) catalyzes the first step of lipid A biosynthesis, the reversible transfer of the R-3-hydroxyacyl chain from R-3-hydroxyacyl acyl carrier protein to the glucosamine 3-OH group of UDP-GlcNAc. Escherichia coli LpxA is highly selective for R-3-hydroxymyristate. The crystal structure of the E. coli LpxA homotrimer, determined previously in the absence of lipid substrates or products, revealed that LpxA contains an unusual, left-handed parallel beta-helix fold. We have now solved the crystal structures of E. coli LpxA with the bound product UDP-3-O-(R-3-hydroxymyristoyl)-GlcNAc at a resolution of 1.74 A and with bound UDP-3-O-(R-3-hydroxydecanoyl)-GlcNAc at 1.85 A. The structures of these complexes are consistent with the catalytic mechanism deduced by mutagenesis and with a recent 3.0-A structure of LpxA with bound UDP-GlcNAc. Our structures show how LpxA selects for 14-carbon R-3-hydroxyacyl chains and reveal two modes of UDP binding.
Indexed as
Identifiers
What OpenQuestion holds
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.