Journal article
Intrinsically disordered protein threads through the bacterial outer-membrane porin OmpF.
- Abstract:
-
Porins are β-barrel outer-membrane proteins through which small solutes and metabolites diffuse that are also exploited during cell death. We have studied how the bacteriocin colicin E9 (ColE9) assembles a cytotoxic translocon at the surface of Escherichia coli that incorporates the trimeric porin OmpF. Formation of the translocon involved ColE9's unstructured N-terminal domain threading in opposite directions through two OmpF subunits, capturing its target TolB on the other side of the membr...
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- Publication status:
- Published
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- Publisher copy:
- 10.1126/science.1237864
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Authors
Bibliographic Details
- Journal:
- Science (New York, N.Y.)
- Volume:
- 340
- Issue:
- 6140
- Pages:
- 1570-1574
- Publication date:
- 2013-06-01
- DOI:
- EISSN:
-
1095-9203
- ISSN:
-
0036-8075
- Source identifiers:
-
410092
Item Description
- Language:
- English
- Keywords:
- Pubs id:
-
pubs:410092
- UUID:
-
uuid:3772ea28-53d8-4b36-b2c9-7d10ea853925
- Local pid:
- pubs:410092
- Deposit date:
- 2013-11-16
Terms of use
- Copyright date:
- 2013
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