ArticleScientific reports2016
Crystal Structure of Escherichia coli originated MCR-1, a phosphoethanolamine transferase for Colistin Resistance.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.
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Who cites it
53 citing papers in PubMed, 102 citations in OpenAlex.
- Bacteriocins in Veterinary Medicine: From Antibiotic Limitations to Targeted Solutions.International journal of molecular sciences · 2026Review
- Asymptomatic faecal carriage of multidrug-resistant and carbapenemase-producing Gram-negative bacteria among inpatients and outpatients in a Kenyan county referral hospital: a cross-sectional study.BMC infectious diseases · 2026Article
- mcr gene family evolution and structural mechanisms of colistin resistance: from mcr-1 to emerging variants.Archives of microbiology · 2026Review
- Mechanistic basis of antimicrobial resistance mediated by the phosphoethanolamine transferase MCR-1.Nature communications · 2025Article
- Colistin resistance in the era of antimicrobial resistance: challenges and strategic countermeasures.Folia microbiologica · 2025Review
- An Evaluation of Alternative Treatment Strategies in Mitigating Colistin Resistance: Targeting Plasmid Transfer Through the Use of Bambermycin or the Protein Coded by the Mcr-1 Gene With Antibodies and Streptomycin.Veterinary medicine and science · 2025Article
- Dynamic Behavior and Substrate Interactions of the Polymyxin Resistance Determinant MCR-1 Investigated by Molecular Dynamics Simulations in the Membrane Environment.Journal of chemical information and modeling · 2025Article
- One Health at Risk: Plasmid-Mediated Spread ofAntibiotics (Basel, Switzerland) · 2025Review
- In vitro synergistic effects of mefloquine combined with other antimicrobial agents on carbapenem-resistant Enterobacterales.European journal of clinical microbiology & infectious diseases : official publication of the European Society of Clinical Microbiology · 2025Article
- Artesunate, EDTA, and colistin work synergistically against MCR-negative and -positive colistin-resistanteLife · 2025Article
- Bacteria carrying mobile colistin resistance genes and their control measures, an updated review.Archives of microbiology · 2024Review
- Article
- A Review on Colistin Resistance: An Antibiotic of Last Resort.Microorganisms · 2024Review
- Structural biology of MCR-1-mediated resistance to polymyxin antibiotics.Current opinion in structural biology · 2023Review
- Cationic Polymers Enable Internalization of Negatively Charged Chemical Probes into Bacteria.ACS chemical biology · 2023Article
- Untying the anchor for the lipopolysaccharide: lipid A structural modification systems offer diagnostic and therapeutic options to tackle polymyxin resistance.Arhiv za higijenu rada i toksikologiju · 2023Review
- Phosphoethanolamine Transferases as Drug Discovery Targets for Therapeutic Treatment of Multi-Drug Resistant Pathogenic Gram-Negative Bacteria.Antibiotics (Basel, Switzerland) · 2023Review
- A Single Residue within the MCR-1 Protein Confers Anticipatory Resilience.Microbiology spectrum · 2023Article
- Gold drugs as colistin adjuvants in the fight against MCR-1 producing bacteria.Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry · 2023Article
- Characterization of two novel colistin resistance geneFrontiers in microbiology · 2023Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
MCR-1 is a phosphoethanolamine (pEtN) transferase that modifies the pEtN moiety of lipid A, conferring resistance to colistin, which is an antibiotic belonging to the class of polypeptide antibiotics known as polymyxins and is the last-line antibiotic used to treat multidrug resistant bacterial infections. Here we determined the crystal structure of the catalytic domain of MCR-1 (MCR-1-ED), which is originated in Escherichia coli (E. coli). MCR-1-ED was found to comprise several classical β-α-β-α motifs that constitute a "sandwich" conformation. Two interlaced molecules with different phosphorylation status of the residue T285 could give rise to two functional statuses of MCR-1 depending on the physiological conditions. MCR-1, like other known pEtN transferases, possesses an enzymatic site equipped with zinc binding residues. Interestingly, two zinc ions were found to mediate intermolecular interactions between MCR-1-ED molecules in one asymmetric unit and hence concatenation of MCR-1, allowing the protein to be oligomer. Findings of this work shall provide important insight into development of effective and clinically useful inhibitors of MCR-1 or structurally similar enzymes.
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