ArticleThe Journal of biological chemistry2011
Structural basis for microcin C7 inactivation by the MccE acetyltransferase.
Article in The Journal of biological chemistry, 2011. 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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Who cites it
19 citing papers in PubMed, 30 citations in OpenAlex.
- Intracellularly driven chemical modifications of antimicrobial secondary metabolites: Potent mechanisms of self-resistance.Pharmaceutical science advances · 2024Review
- Decarboxylation in Natural Products Biosynthesis.JACS Au · 2024Review
- An evolutionary history of the CoA-binding protein Nat/Ivy.Protein science : a publication of the Protein Society · 2022Review
- Article
- Natural Trojan horse inhibitors of aminoacyl-tRNA synthetases.RSC chemical biology · 2021Review
- Gcn5-RelatedFrontiers in molecular biosciences · 2021Article
- Small-Molecule Acetylation by GCN5-RelatedMicrobiology and molecular biology reviews : MMBR · 2020Review
- Bacteriocins to Thwart Bacterial Resistance in Gram Negative Bacteria.Frontiers in microbiology · 2020Review
- Translation-Targeting RiPPs and Where to Find Them.Frontiers in genetics · 2020Review
- Article
- Biosynthesis of the RiPP trojan horse nucleotide antibiotic microcin C is directed by theChemical science · 2019Article
- Natural Products Containing 'Rare' Organophosphorus Functional Groups.Molecules (Basel, Switzerland) · 2019Review
- Microcins inFrontiers in microbiology · 2019Review
- Comparison of Strategies to Overcome Drug Resistance: Learning from Various Kingdoms.Molecules (Basel, Switzerland) · 2018Review
- Structure and Functional Diversity of GCN5-Related N-Acetyltransferases (GNAT).International journal of molecular sciences · 2016Review
- Bacterial GCN5-Related N-Acetyltransferases: From Resistance to Regulation.Biochemistry · 2016Review
- Article
- The RimL transacetylase provides resistance to translation inhibitor microcin C.Journal of bacteriology · 2014Article
- Microcin C: biosynthesis and mechanisms of bacterial resistance.Future microbiology · 2012Review
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The antibiotic microcin C7 (McC) acts as a bacteriocide by inhibiting aspartyl-tRNA synthetase and stalling the protein translation machinery. McC is synthesized as a heptapeptide-nucleotide conjugate, which is processed by cellular peptidases within target strains to yield the biologically active compound. As unwanted processing of intact McC can result in self-toxicity, producing strains utilize multiple mechanisms for autoimmunity against processed McC. We have shown previously that the mccE gene within the biosynthetic cluster can inactivate processed McC by acetylating the antibiotic. Here, we present the characterization of this acetylation mechanism through biochemical and structural biological studies of the MccE acetyltransferase domain (MccE(AcTase)). We have also determined five crystal structures of the MccE-acetyl-CoA complex with bound substrates, inhibitor, and reaction product. The structural data reveal an unexpected mode of substrate recognition through π-stacking interactions similar to those found in cap-binding proteins and nucleotidyltransferases. These studies provide a rationale for the observation that MccE(AcTase) can detoxify a range of aminoacylnucleotides, including those that are structurally distinct from microcin C7.
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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.