ArticleJournal of molecular biology2012
Structural and functional characterization of microcin C resistance peptidase MccF from Bacillus anthracis.
Article in Journal of molecular biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 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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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
19 citing papers in PubMed, 25 citations in OpenAlex.
- Genes and physiological strategies in bacterial antibiotic resistance.Frontiers in microbiology · 2026Review
- Ribosomally Synthesized and Post-Translationally Modified Peptides Assembled by ThiF-like Adenylyltransferases: Recent Advances and Future Perspectives.Molecules (Basel, Switzerland) · 2025Review
- Bacterial interactions on nutrient-rich surfaces in the gut lumen.Infection and immunity · 2024Review
- Microalgae and Bacteria Interaction-Evidence for Division of Diligence in the Alga Microbiota.Microbiology spectrum · 2022Article
- Natural Trojan horse inhibitors of aminoacyl-tRNA synthetases.RSC chemical biology · 2021Review
- Bacteriocins as a new generation of antimicrobials: toxicity aspects and regulations.FEMS microbiology reviews · 2021Review
- Modulation of Peptidoglycan Synthesis by Recycled Cell Wall Tetrapeptides.Cell reports · 2020Article
- Bacteriocins, Antimicrobial Peptides from Bacterial Origin: Overview of Their Biology and Their Impact against Multidrug-Resistant Bacteria.Microorganisms · 2020Review
- Progress and challenges in aminoacyl-tRNA synthetase-based therapeutics.The Journal of biological chemistry · 2019Review
- Microcins inFrontiers in microbiology · 2019Review
- Antibiotics, Resistome and Resistance Mechanisms: A Bacterial Perspective.Frontiers in microbiology · 2018Review
- Biofilm formation and transcriptome analysis of Streptococcus gallolyticus subsp. gallolyticus in response to lysozyme.PloS one · 2018Article
- Broad Analysis of Vicinal Disulfides: Occurrences, Conformations with Cis or with Trans Peptides, and Functional Roles Including Sugar Binding.Journal of molecular biology · 2017Article
- A Trojan-Horse Peptide-Carboxymethyl-Cytidine Antibiotic from Bacillus amyloliquefaciens.Journal of the American Chemical Society · 2016Article
- Single-residue posttranslational modification sites at the N-terminus, C-terminus or in-between: To be or not to be exposed for enzyme access.Proteomics · 2015Article
- Antibiotic alternatives: the substitution of antibiotics in animal husbandry?Frontiers in microbiology · 2014Review
- Antibiotic development challenges: the various mechanisms of action of antimicrobial peptides and of bacterial resistance.Frontiers in microbiology · 2013Review
- Structure and function of a novel LD-carboxypeptidase a involved in peptidoglycan recycling.Journal of bacteriology · 2013Article
- Bacteriocins - a viable alternative to antibiotics?Nature reviews. Microbiology · 2013Review
Corrections and comments
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Authors and funding
12 authors at 6 institutions in 3 countries.
Funding
Abstract
Microcin C (McC) is heptapeptide adenylate antibiotic produced by Escherichia coli strains carrying the mccABCDEF gene cluster encoding enzymes, in addition to the heptapeptide structural gene mccA, necessary for McC biosynthesis and self-immunity of the producing cell. The heptapeptide facilitates McC transport into susceptible cells, where it is processed releasing a non-hydrolyzable aminoacyl adenylate that inhibits an essential aminoacyl-tRNA synthetase. The self-immunity gene mccF encodes a specialized serine peptidase that cleaves an amide bond connecting the peptidyl or aminoacyl moieties of, respectively, intact and processed McC with the nucleotidyl moiety. Most mccF orthologs from organisms other than E. coli are not linked to the McC biosynthesis gene cluster. Here, we show that a protein product of one such gene, MccF from Bacillus anthracis (BaMccF), is able to cleave intact and processed McC, and we present a series of structures of this protein. Structural analysis of apo-BaMccF and its adenosine monophosphate complex reveals specific features of MccF-like peptidases that allow them to interact with substrates containing nucleotidyl moieties. Sequence analyses and phylogenetic reconstructions suggest that several distinct subfamilies form the MccF clade of the large S66 family of bacterial serine peptidases. We show that various representatives of the MccF clade can specifically detoxify non-hydrolyzable aminoacyl adenylates differing in their aminoacyl moieties. We hypothesize that bacterial mccF genes serve as a source of bacterial antibiotic resistance.
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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.