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Single-molecule investigation of directional transport through a bacterial transmembrane pore

Abstract:
Colicin E9 (ColE9) crosses the outer membrane of E. coli by passing through the trimeric OmpF porin. Entry is initiated by an intrinsically unstructured N-terminal domain (IUTD), which has two OmpF-binding sites (OBS). The IUTD threads through a first subunit of OmpF, reverses direction and enters a second subunit, leaving the IUTD sequence OBS2 within the first subunit, OBS1 within the second subunit and the intervening TolB-binding epitope in the periplasmic space.
Publication status:
Published
Peer review status:
Reviewed (other)

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Publisher copy:
10.1007/s00249-017-1222-x

Authors


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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; Chemical Biology
Role:
Author
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
Department:
Chemistry
Sub department:
Chemical Biology
Role:
Author
Publisher:
Springer Publisher's website
Journal:
19th IUPAB Congress and 11th EBSA Congress Journal website
Host title:
9th IUPAB Congress and 11th EBSA Congresss
Publication date:
2017-06-26
Acceptance date:
2017-07-16
DOI:
ISSN:
1432-1017 and 0175-7571
Source identifiers:
813576
Pubs id:
pubs:813576
UUID:
uuid:1448765f-c100-42c0-9e2e-d4db5b2b86ef
Local pid:
pubs:813576
Deposit date:
2018-06-27

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