ArticleThe Journal of biological chemistry2008
Crystal structure of colicin M, a novel phosphatase specifically imported by Escherichia coli.
Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.
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Who cites it
34 citing papers in PubMed, 64 citations in OpenAlex.
- Substrate Uptake by TonB-Dependent Outer Membrane Transporters.Molecular microbiology · 2024Review
- Crystal structure of pectocin M1 reveals diverse conformations and interactions during its initial step via the ferredoxin uptake system.FEBS open bio · 2024Article
- Story of Pore-Forming Proteins from Deadly Disease-Causing Agents to Modern Applications with Evolutionary Significance.Molecular biotechnology · 2024Review
- Trojan horselike T6SS effector TepC mediates both interference competition and exploitative competition.The ISME journal · 2024Article
- A secreted effector with a dual role as a toxin and as a transcriptional factor.Nature communications · 2022Article
- The Biology of Colicin M and Its Orthologs.Antibiotics (Basel, Switzerland) · 2021Review
- CbrA Mediates Colicin M Resistance in Escherichia coli through Modification of Undecaprenyl-Phosphate-Linked Peptidoglycan Precursors.Journal of bacteriology · 2020Article
- Polymorphic Toxins and Their Immunity Proteins: Diversity, Evolution, and Mechanisms of Delivery.Annual review of microbiology · 2020Review
- Comparative Genomic Analysis Provides Insights into the Phylogeny, Resistome, Virulome, and Host Adaptation in the GenusPathogens (Basel, Switzerland) · 2020Article
- Impact of FiuA Outer Membrane Receptor Polymorphism on the Resistance ofJournal of bacteriology · 2019Article
- Article
- A Natural ChimericmBio · 2017Article
- Discovery, characterization and in vivo activity of pyocin SD2, a protein antibiotic from Pseudomonas aeruginosa.The Biochemical journal · 2016Article
- Protein folding in the cell envelope of Escherichia coli.Nature microbiology · 2016Review
- Structure of the atypical bacteriocin pectocin M2 implies a novel mechanism of protein uptake.Molecular microbiology · 2014Article
- Daring to be different: colicin N finds another way.Molecular microbiology · 2014Article
- Lectin-like bacteriocins from Pseudomonas spp. utilise D-rhamnose containing lipopolysaccharide as a cellular receptor.PLoS pathogens · 2014Article
- Cell Wall-active Bacteriocins and Their Applications Beyond Antibiotic Activity.Probiotics and antimicrobial proteins · 2012Article
- The crystal structure of the lipid II-degrading bacteriocin syringacin M suggests unexpected evolutionary relationships between colicin M-like bacteriocins.The Journal of biological chemistry · 2012Article
- Functional and structural characterization of PaeM, a colicin M-like bacteriocin produced by Pseudomonas aeruginosa.The Journal of biological chemistry · 2012Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Colicins are cytotoxic proteins secreted by certain strains of Escherichia coli. Colicin M is unique among these toxins in that it acts in the periplasm and specifically inhibits murein biosynthesis by hydrolyzing the pyrophosphate linkage between bactoprenol and the murein precursor. We crystallized colicin M and determined the structure at 1.7A resolution using x-ray crystallography. The protein has a novel structure composed of three domains with distinct functions. The N-domain is a short random coil and contains the exposed TonB box. The central domain includes a hydrophobic alpha-helix and binds presumably to the FhuA receptor. The C-domain is composed of a mixed alpha/beta-fold and forms the phosphatase. The architectures of the individual modules show no similarity to known structures. Amino acid replacements in previously isolated inactive colicin M mutants are located in the phosphatase domain, which contains a number of surface-exposed residues conserved in predicted bacteriocins of other bacteria. The novel phosphatase domain displays no sequence similarity to known phosphatases. The N-terminal and central domains are not conserved among bacteriocins, which likely reflect the distinct import proteins required for the uptake of the various bacteriocins. The homology pattern supports our previous proposal that colicins evolved by combination of distinct functional domains.
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