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

Grinter, R; Josts, I; Zeth, K; Roszak, AW; Mccaughey, LC; Cogdell, RJ; Milner, JJ; Kelly, SM; Byron, O; Walker, D

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

Grinter, R Josts, I Zeth, K Roszak, AW Mccaughey, LC

Cogdell, RJ Milner, JJ Kelly, SM Byron, O Walker, D

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Publication Type:: Journal Article
Citation:: Molecular Microbiology, 2014, 93 (2), pp. 234 - 246
Issue Date:: 2014-01-01

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Field	Value	Language
dc.contributor.author	Grinter, R	en_US
dc.contributor.author	Josts, I	en_US
dc.contributor.author	Zeth, K	en_US
dc.contributor.author	Roszak, AW	en_US
dc.contributor.author	Mccaughey, LC https://orcid.org/0000-0001-5897-0163	en_US
dc.contributor.author	Cogdell, RJ	en_US
dc.contributor.author	Milner, JJ	en_US
dc.contributor.author	Kelly, SM	en_US
dc.contributor.author	Byron, O	en_US
dc.contributor.author	Walker, D	en_US
dc.date.available	2014-05-23	en_US
dc.date.issued	2014-01-01	en_US
dc.identifier.citation	Molecular Microbiology, 2014, 93 (2), pp. 234 - 246	en_US
dc.identifier.issn	0950-382X	en_US
dc.identifier.uri	http://hdl.handle.net/10453/116035
dc.description.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. © 2014 The Authors. Molecular Microbiology published by John Wiley & Sons Ltd.	en_US
dc.relation.ispartof	Molecular Microbiology	en_US
dc.relation.isbasedon	10.1111/mmi.12655	en_US
dc.subject.classification	Microbiology	en_US
dc.subject.mesh	Pectobacterium	en_US
dc.subject.mesh	Iron	en_US
dc.subject.mesh	Muramidase	en_US
dc.subject.mesh	Bacteriocins	en_US
dc.subject.mesh	Colicins	en_US
dc.subject.mesh	Ferredoxins	en_US
dc.subject.mesh	Crystallization	en_US
dc.subject.mesh	Crystallography, X-Ray	en_US
dc.subject.mesh	Amino Acid Sequence	en_US
dc.subject.mesh	Protein Conformation	en_US
dc.subject.mesh	Protein Structure, Tertiary	en_US
dc.subject.mesh	Protein Transport	en_US
dc.subject.mesh	Models, Molecular	en_US
dc.subject.mesh	Molecular Sequence Data	en_US
dc.title	Structure of the atypical bacteriocin pectocin M2 implies a novel mechanism of protein uptake	en_US
dc.type	Journal Article
utslib.citation.volume	2	en_US
utslib.citation.volume	93	en_US
utslib.for	0605 Microbiology	en_US
utslib.for	06 Biological Sciences	en_US
utslib.for	07 Agricultural and Veterinary Sciences	en_US
utslib.for	11 Medical and Health Sciences	en_US
pubs.embargo.period	Not known	en_US
pubs.organisational-group	/University of Technology Sydney
pubs.organisational-group	/University of Technology Sydney/Faculty of Science
pubs.organisational-group	/University of Technology Sydney/Strength - ithree - Institute of Infection, Immunity and Innovation
utslib.copyright.status	open_access
pubs.issue	2	en_US
pubs.publication-status	Published	en_US
pubs.volume	93	en_US

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. © 2014 The Authors. Molecular Microbiology published by John Wiley & Sons Ltd.

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http://hdl.handle.net/10453/116035