ArticleMolecular microbiology2014
Structure of the atypical bacteriocin pectocin M2 implies a novel mechanism of protein uptake.
Article in Molecular microbiology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 35 citations in OpenAlex.
- Crystal structure of pectocin M1 reveals diverse conformations and interactions during its initial step via the ferredoxin uptake system.FEBS open bio · 2024Article
- The Evolutionary History of Peptidases Involved in the Processing of Organelle-Targeting Peptides.Genome biology and evolution · 2022Article
- Heterologous overexpression and preliminary antimicrobial activity test of salmocin M, a novel colicin M-like bacteriocin against Salmonella sp.Archives of microbiology · 2022Article
- The Biology of Colicin M and Its Orthologs.Antibiotics (Basel, Switzerland) · 2021Review
- Anticancer and antimicrobial potential of enterocin 12a from Enterococcus faecium.BMC microbiology · 2021Article
- Article
- The crystal structure of the TonB-dependent transporter YncD reveals a positively charged substrate-binding site.Acta crystallographica. Section D, Structural biology · 2020Article
- Bacteriocins Targeting Gram-Negative Phytopathogenic Bacteria: Plantibiotics of the Future.Frontiers in microbiology · 2020Review
- The structure of the bacterial iron-catecholate transporter Fiu suggests that it imports substrates via a two-step mechanism.The Journal of biological chemistry · 2019Article
- Protease-associated import systems are widespread in Gram-negative bacteria.PLoS genetics · 2019Article
- Impact of FiuA Outer Membrane Receptor Polymorphism on the Resistance ofJournal of bacteriology · 2019Article
- Article
- FusC, a member of the M16 protease family acquired by bacteria for iron piracy against plants.PLoS biology · 2018Article
- Bacterial iron acquisition mediated by outer membrane translocation and cleavage of a host protein.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Article
- The Two-State Prehensile Tail of the Antibacterial Toxin Colicin N.Biophysical journal · 2017Article
- Novel Immunity Proteins Associated with Colicin M-like Bacteriocins Exhibit Promiscuous Protection inFrontiers in microbiology · 2017Article
- Structure of the bacterial plant-ferredoxin receptor FusA.Nature communications · 2016Article
- Pectocin M1 (PcaM1) Inhibits Escherichia coli Cell Growth and Peptidoglycan Biosynthesis through Periplasmic Expression.Antibiotics (Basel, Switzerland) · 2016Article
- Antibacterial toxin colicin N and phage protein G3p compete with TolB for a binding site on TolA.Microbiology (Reading, England) · 2015Article
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Authors and funding
10 authors at 3 institutions in 3 countries.
Funding
Abstract
The colicin-like bacteriocins are potent protein antibiotics that have evolved to efficiently cross the outer membrane of Gram-negative bacteria by parasitizing nutrient uptake systems. We have structurally characterized the colicin M-like bacteriocin, pectocin M2, which is active against strains of Pectobacterium spp. This unusual bacteriocin lacks the intrinsically unstructured translocation domain that usually mediates translocation of these bacteriocins across the outer membrane, containing only a single globular ferredoxin domain connected to its cytotoxic domain by a flexible α-helix, which allows it to adopt two distinct conformations in solution. The ferredoxin domain of pectocin M2 is homologous to plant ferredoxins and allows pectocin M2 to parasitize a system utilized by Pectobacterium to obtain iron during infection of plants. Furthermore, we identify a novel ferredoxin-containing bacteriocin pectocin P, which possesses a cytotoxic domain homologous to lysozyme, illustrating that the ferredoxin domain acts as a generic delivery module for cytotoxic domains in Pectobacterium.
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