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Clusters in an intrinsically disordered protein create a protein-binding site: the TolB-binding region of colicin E9.

Abstract:

The 61-kDa colicin E9 protein toxin enters the cytoplasm of susceptible cells by interacting with outer membrane and periplasmic helper proteins and kills them by hydrolyzing their DNA. The membrane translocation function is located in the N-terminal domain of the colicin, with a key signal sequence being a pentapeptide region that governs the interaction with the helper protein TolB (the TolB box). Previous NMR studies [Collins et al. (2002) J. Mol. Biol. 318, 787-904; MacDonald et al. (2004...

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Publisher copy:
10.1021/bi0503596

Authors


Macdonald, CJ More by this author
Penfold, CN More by this author
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Institution:
University of Oxford
Department:
Oxford, MSD, Biochemistry
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Journal:
Biochemistry
Volume:
44
Issue:
34
Pages:
11496-11507
Publication date:
2005-08-05
DOI:
EISSN:
1520-4995
ISSN:
0006-2960
URN:
uuid:c221ba16-aa80-407e-989c-2abac9f47c26
Source identifiers:
310227
Local pid:
pubs:310227

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