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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

Authors


Housden, NG More by this author
Hopper, JT More by this author
Lukoyanova, N More by this author
Rodriguez-Larrea, D More by this author
Wojdyla, JA More by this author
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Journal:
Science (New York, N.Y.)
Volume:
340
Issue:
6140
Pages:
1570-1574
Publication date:
2013-06-05
DOI:
EISSN:
1095-9203
ISSN:
0036-8075
URN:
uuid:3772ea28-53d8-4b36-b2c9-7d10ea853925
Source identifiers:
410092
Local pid:
pubs:410092

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