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Journal article

Directional porin binding of intrinsically disordered protein sequences promotes colicin epitope display in the bacterial periplasm

Abstract:

Protein bacteriocins are potent narrow spectrum antibiotics that exploit outer membrane porins to kill bacteria by poorly understood mechanisms. Here, we determine how colicins, bacteriocins specific for Escherichia coli, engage the trimeric porin OmpF to initiate toxin entry. The N-terminal ∼80 residues of the nuclease colicin ColE9 are intrinsically unstructured and house two OmpF binding sites (OBS1 and OBS2) that reside within the pores of OmpF and which flank an epitope that binds peripl...

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Publication status:
Published
Peer review status:
Peer reviewed
Version:
Publisher's version

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Publisher copy:
10.1021/acs.biochem.8b00621

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Institution:
University of Oxford
Division:
Medical Sciences Division
Department:
Biochemistry
Role:
Author
ORCID:
0000-0002-4706-8278
More by this author
Institution:
University of Oxford
Division:
Medical Sciences Division
Department:
Biochemistry
Role:
Author
More by this author
Institution:
University of Oxford
Division:
MPLS Division
Department:
Chemistry
Role:
Author
More by this author
Institution:
University of Oxford
Division:
Medical Sciences Division
Department:
Biochemistry
Role:
Author
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Publisher:
American Chemical Society Publisher's website
Journal:
Biochemistry Journal website
Volume:
57
Issue:
29
Pages:
4374–4381
Publication date:
2018-06-27
Acceptance date:
2018-06-27
DOI:
EISSN:
1520-4995
ISSN:
0006-2960
Pubs id:
pubs:859814
URN:
uri:acbefcb8-aef2-4156-8c9a-9e6dc355ce93
UUID:
uuid:acbefcb8-aef2-4156-8c9a-9e6dc355ce93
Local pid:
pubs:859814
Language:
English

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