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Structure of the atypical bacteriocin pectocin M2 implies a novel mechanism of protein uptake

DOI: 10.1111/mmi.12655 DOI Help
PMID: 24865810 PMID Help

Authors: Rhys Grinter (Institute of Infection, Immunity and Inflammation, University of Glasgow) , Inokentijs Josts (Institute of Infection, Immunity and Inflammation, University of Glasgow) , Kornelius Zeth (Unidad de Biofisica (CSIC-UPV/EHU), Vizcaya) , Aleksander Roszak (WestCHEM, School of Chemistry, College of Science and Engineering, University of Glasgow) , Laura C. Mccaughey (Institute of Infection, Immunity and Inflammation, University of Glasgow) , Richard J. Cogdell (Institute of Molecular Cell and Systems Biology, University of Glasgow) , Joel J. Milner (School of Life Sciences, College of Medical, Veterinary and Life Sciences, University of Glasgow) , Sharon Kelly (Institute of Molecular Cell and Systems Biology, University of Glasgow) , Olwyn Byron (School of Life Sciences, College of Medical, Veterinary and Life Sciences, University of Glasgow) , Daniel Walker (Institute of Infection, Immunity and Inflammation, University of Glasgow)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Molecular Microbiology , VOL 93 (2) , PAGES 234 - 246

State: Published (Approved)
Published: July 2014
Diamond Proposal Number(s): 6638 , 8659

Open Access Open Access

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.

Subject Areas: Biology and Bio-materials


Instruments: I02-Macromolecular Crystallography , I03-Macromolecular Crystallography