ArticleProceedings of the National Academy of Sciences of the United States of America2006
Structure of UDP-N-acetylglucosamine acyltransferase with a bound antibacterial pentadecapeptide.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
What it found
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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.
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Who cites it
35 citing papers in PubMed.
- Lipase and Protease Production Ability of Multi-drug Resistant Bacteria Worsens the Outcomes of Wound Infections.Current pharmaceutical design · 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
- Phage Display-Derived Peptides and Antibodies for Bacterial Infectious Diseases Therapy and Diagnosis.Molecules (Basel, Switzerland) · 2023Review
- Targeting LPS biosynthesis and transport in gram-negative bacteria in the era of multi-drug resistance.Biochimica et biophysica acta. Molecular cell research · 2023Review
- Identification and prioritization of potential therapeutic molecules against LpxA fromCurrent research in structural biology · 2023Article
- Computer-Based Identification of Potential Druggable Targets in Multidrug-ResistantMicroorganisms · 2022Article
- Pathway Driven Target Selection inFrontiers in cellular and infection microbiology · 2022Article
- Using Structure-guided Fragment-Based Drug Discovery to TargetFrontiers in molecular biosciences · 2022Review
- Malonyl-acyl carrier protein decarboxylase activity promotes fatty acid and cell envelope biosynthesis in Proteobacteria.The Journal of biological chemistry · 2021Article
- Essential Genes ofFrontiers in microbiology · 2021Article
- Article
- 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
- Non-steric-zipper models for pathogenic α-synuclein conformers.APL bioengineering · 2018Article
- Crystal structure of lipid A disaccharide synthase LpxB from Escherichia coli.Nature communications · 2018Article
- Structure, inhibition, and regulation of essential lipid A enzymes.Biochimica et biophysica acta. Molecular and cell biology of lipids · 2017Review
- Crystal structure and activity of Francisella novicida UDP-N-acetylglucosamine acyltransferase.Biochemical and biophysical research communications · 2016Article
- Structural basis for the recognition of peptide RJPXD33 by acyltransferases in lipid A biosynthesis.The Journal of biological chemistry · 2014Article
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
UDP-GlcNAc acyltransferase (LpxA) catalyzes the first step of lipid A biosynthesis, the transfer of the R-3-hydroxyacyl chain from R-3-hydroxyacyl acyl carrier protein (ACP) to the glucosamine 3-OH group of UDP-GlcNAc. LpxA is essential for the growth of Escherichia coli and related Gram-negative bacteria. The crystal structure of the E. coli LpxA homotrimer, determined previously at 2.6 A in the absence of substrates or inhibitors, revealed that LpxA contains an unusual, left-handed parallel beta-helix fold. We now present the crystal structure at 1.8 A resolution of E. coli LpxA in a complex with a pentadecapeptide, peptide 920. Three peptides, each of which adopts a beta-hairpin conformation, are bound per LpxA trimer. The peptides are located at the interfaces of adjacent subunits in the vicinity of the three active sites. Each peptide interacts with residues from both adjacent subunits. Peptide 920 is a potent inhibitor of E. coli LpxA (Ki = 50 nM). It is competitive with respect to acyl-ACP but not UDP-GlcNAc. The compact beta-turn structure of peptide 920 bound to LpxA may open previously uncharacterized approaches to the rational design of LpxA inhibitors with antibiotic activity.
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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.