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Characterisation of a mobile protein-binding epitope in the translocation domain 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 hydrolysing 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, 787-804) have shown that the N-...

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Journal:
Journal of biomolecular NMR
Volume:
30
Issue:
1
Pages:
81-96
Publication date:
2004-09-05
DOI:
EISSN:
1573-5001
ISSN:
0925-2738
URN:
uuid:fe8f6d06-33ff-446a-a7eb-893b7af567a9
Source identifiers:
310230
Local pid:
pubs:310230

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