ArticleScience (New York, N.Y.)2016
Structures of aminoarabinose transferase ArnT suggest a molecular basis for lipid A glycosylation.
Article in Science (New York, N.Y.), 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 76 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.
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Who cites it
76 citing papers in PubMed, 118 citations in OpenAlex.
- Structures of ALG3/9/12 reveal the assembly logic of the N-glycan oligomannose core.Nature chemical biology · 2026Article
- A posttranslational modification of fimbriae drives pathogenicity inProceedings of the National Academy of Sciences of the United States of America · 2026Article
- Article
- Exploration of the aromatic abietane diterpenoid scaffold in the development of ArnT-mediated colistin resistance inhibitors.RSC advances · 2026Article
- Natural compounds: a promising therapeutic option for managing colistin-resistant bacteria and improving colistin activity.Molecular biology reports · 2026Review
- Molecular mechanisms of disinfectant resistance inJAC-antimicrobial resistance · 2026Article
- Polymyxin resistance in Gram-negative bacteria: a comprehensive review with a focus on the role of 4-amino-4-doexy-L-arabinose.Molecular biology reports · 2025Review
- Structural basis of undecaprenyl phosphate glycosylation leading to polymyxin resistance in Gram-negative bacteria.Nature communications · 2025Article
- Mechanistic basis of antimicrobial resistance mediated by the phosphoethanolamine transferase MCR-1.Nature communications · 2025Article
- Ionomer engineering for optimized water channels in industry-scale water electrolysis using non-noble metal catalyst.Nature communications · 2025Article
- Structural Basis for Targeting the Bifunctional Enzyme ArnA.Biomolecules · 2025Article
- A novel post-translational modification of fimbriae drives pathogenicity inbioRxiv : the preprint server for biology · 2025Article
- Mechanistic studies of mycobacterial glycolipid biosynthesis by the mannosyltransferase PimE.Nature communications · 2025Article
- Structural insights into terminal arabinosylation of mycobacterial cell wall arabinan.Nature communications · 2025Article
- Structural insights into polyisoprenyl-binding glycosyltransferases.Structure (London, England : 1993) · 2025Review
- Structural glycobiology - from enzymes to organelles.Biochemical Society transactions · 2025Review
- More than one way to add a sugar into bacterial polysaccharides.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Three-component systems represent a common pathway for extracytoplasmic addition of pentofuranose sugars into bacterial glycans.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- The Effect of the PhoP/PhoQ System on the Regulation of Multi-Stress Adaptation Induced by Acid Stress inFoods (Basel, Switzerland) · 2024Article
- Upregulation of outer membrane porin geneMicrobiology spectrum · 2024Article
16 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
16 authors at 4 institutions in 1 country.
Funding
Abstract
Polymyxins are antibiotics used in the last line of defense to combat multidrug-resistant infections by Gram-negative bacteria. Polymyxin resistance arises through charge modification of the bacterial outer membrane with the attachment of the cationic sugar 4-amino-4-deoxy-l-arabinose to lipid A, a reaction catalyzed by the integral membrane lipid-to-lipid glycosyltransferase 4-amino-4-deoxy-L-arabinose transferase (ArnT). Here, we report crystal structures of ArnT from Cupriavidus metallidurans, alone and in complex with the lipid carrier undecaprenyl phosphate, at 2.8 and 3.2 angstrom resolution, respectively. The structures show cavities for both lipidic substrates, which converge at the active site. A structural rearrangement occurs on undecaprenyl phosphate binding, which stabilizes the active site and likely allows lipid A binding. Functional mutagenesis experiments based on these structures suggest a mechanistic model for ArnT family enzymes.
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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.