ArticleActa crystallographica. Section D, Biological crystallography2014
Crystallographic study of the phosphoethanolamine transferase EptC required for polymyxin resistance and motility in Campylobacter jejuni.
Article in Acta crystallographica. Section D, Biological crystallography, 2014. 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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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
26 citing papers in PubMed, 39 citations in OpenAlex.
- Mechanistic basis of antimicrobial resistance mediated by the phosphoethanolamine transferase MCR-1.Nature communications · 2025Article
- Epigenetic modulation of Ceratorhiza hydrophila by 5-azacytidine enhances antifungal metabolite production: insights from antimicrobial, metabolic, genomic and computational analyses.BMC microbiology · 2025Article
- Article
- The multifaceted roles of phosphoethanolamine-modified lipopolysaccharides: from stress response and virulence to cationic antimicrobial resistance.Microbiology and molecular biology reviews : MMBR · 2024Review
- Structural biology of MCR-1-mediated resistance to polymyxin antibiotics.Current opinion in structural biology · 2023Review
- Phosphoethanolamine Transferases as Drug Discovery Targets for Therapeutic Treatment of Multi-Drug Resistant Pathogenic Gram-Negative Bacteria.Antibiotics (Basel, Switzerland) · 2023Review
- Deciphering the genetic network and programmed regulation of antimicrobial resistance in bacterial pathogens.Frontiers in cellular and infection microbiology · 2022Review
- The bile salt deoxycholate inducesFrontiers in microbiology · 2022Article
- Global epidemiology, genetic environment, risk factors and therapeutic prospects ofFrontiers in cellular and infection microbiology · 2022Review
- The essential inner membrane protein YejM is a metalloenzyme.Scientific reports · 2020Article
- Polymyxins and Bacterial Membranes: A Review of Antibacterial Activity and Mechanisms of Resistance.Membranes · 2020Review
- Recent progress on elucidating the molecular mechanism of plasmid-mediated colistin resistance and drug design.International microbiology : the official journal of the Spanish Society for Microbiology · 2020Review
- An atypical lipoteichoic acid fromThe Journal of biological chemistry · 2020Article
- TheThe Journal of biological chemistry · 2020Article
- Structural and Functional Characterization of the BcsG Subunit of the Cellulose Synthase in Salmonella typhimurium.Journal of molecular biology · 2018Article
- Emergence of High-Level Colistin Resistance in an Acinetobacter baumannii Clinical Isolate Mediated by Inactivation of the Global Regulator H-NS.Antimicrobial agents and chemotherapy · 2018Article
- Substrate Recognition by a Colistin Resistance Enzyme from Moraxella catarrhalis.ACS chemical biology · 2018Article
- Synergistic effect of eugenol with Colistin against clinical isolated Colistin-resistantAntimicrobial resistance and infection control · 2018Article
- Characterization of Two Novel Lipopolysaccharide Phosphoethanolamine Transferases in Pasteurella multocida and Their Role in Resistance to Cathelicidin-2.Infection and immunity · 2017Article
- Novel coordination of lipopolysaccharide modifications in Vibrio cholerae promotes CAMP resistance.Molecular microbiology · 2017Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
The foodborne enteric pathogen Campylobacter jejuni decorates a variety of its cell-surface structures with phosphoethanolamine (pEtN). Modifying lipid A with pEtN promotes cationic antimicrobial peptide resistance, whereas post-translationally modifying the flagellar rod protein FlgG with pEtN promotes flagellar assembly and motility, which are processes that are important for intestinal colonization. EptC, the pEtN transferase required for all known pEtN cell-surface modifications in C. jejuni, is a predicted inner-membrane metalloenzyme with a five-helix N-terminal transmembrane domain followed by a soluble sulfatase-like catalytic domain in the periplasm. The atomic structure of the catalytic domain of EptC (cEptC) was crystallized and solved to a resolution of 2.40 Å. cEptC adopts the α/β/α fold of the sulfatase protein family and harbors a zinc-binding site. A phosphorylated Thr266 residue was observed that was hypothesized to mimic a covalent pEtN-enzyme intermediate. The requirement for Thr266 as well as the nearby residues Asn308, Ser309, His358 and His440 was ascertained via in vivo activity assays on mutant strains. The results establish a basis for the design of pEtN transferase inhibitors.
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