ArticleThe Journal of biological chemistry2012
The crystal structure of the lipid II-degrading bacteriocin syringacin M suggests unexpected evolutionary relationships between colicin M-like bacteriocins.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 41 citations in OpenAlex.
- Pyocins and Beyond: Exploring the World of Bacteriocins in Pseudomonas aeruginosa.Probiotics and antimicrobial proteins · 2025Review
- The potential of bacteriocins and bacteriophages to control bacterial disease of crops with a focus onJournal of the Royal Society of New Zealand · 2025Review
- Crystal structure of pectocin M1 reveals diverse conformations and interactions during its initial step via the ferredoxin uptake system.FEBS open bio · 2024Article
- 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
- Article
- Bacteriocins Targeting Gram-Negative Phytopathogenic Bacteria: Plantibiotics of the Future.Frontiers in microbiology · 2020Review
- Pseudomonas bacteriocin syringacin M released upon desiccation suppresses the growth of sensitive bacteria in plant necrotic lesions.Microbial biotechnology · 2020Article
- Protease-associated import systems are widespread in Gram-negative bacteria.PLoS genetics · 2019Article
- A Colicin M-Type Bacteriocin from Pseudomonas aeruginosa Targeting the HxuC Heme Receptor Requires a Novel Immunity Partner.Applied and environmental microbiology · 2018Article
- Article
- A Natural ChimericmBio · 2017Article
- Use of the Soft-agar Overlay Technique to Screen for Bacterially Produced Inhibitory Compounds.Journal of visualized experiments : JoVE · 2017Article
- Novel Immunity Proteins Associated with Colicin M-like Bacteriocins Exhibit Promiscuous Protection inFrontiers in microbiology · 2017Article
- Article
- 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
- Distinct colicin M-like bacteriocin-immunity pairs in Burkholderia.Scientific reports · 2015Article
- Different Ancestries of R Tailocins in Rhizospheric Pseudomonas Isolates.Genome biology and evolution · 2015Article
- Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Colicin-like bacteriocins show potential as next generation antibiotics with clinical and agricultural applications. Key to these potential applications is their high potency and species specificity that enables a single pathogenic species to be targeted with minimal disturbance of the wider microbial community. Here we present the structure and function of the colicin M-like bacteriocin, syringacin M from Pseudomonas syringae pv. tomato DC3000. Syringacin M kills susceptible cells through a highly specific phosphatase activity that targets lipid II, ultimately inhibiting peptidoglycan synthesis. Comparison of the structures of syringacin M and colicin M reveals that, in addition to the expected similarity between the homologous C-terminal catalytic domains, the receptor binding domains of these proteins, which share no discernible sequence homology, share a striking structural similarity. This indicates that the generation of the novel receptor binding and species specificities of these bacteriocins has been driven by diversifying selection rather than diversifying recombination as suggested previously. Additionally, the structure of syringacin M reveals the presence of an active site calcium ion that is coordinated by a conserved aspartic acid side chain and is essential for catalytic activity. We show that mutation of this residue to alanine inactivates syringacin M and that the metal ion is absent from the structure of the mutant protein. Consistent with the presence of Ca(2+) in the active site, we show that syringacin M activity is supported by Ca(2+), along with Mg(2+) and Mn(2+), and the protein is catalytically inactive in the absence of these ions.
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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.