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Journal article

Flexibility in the receptor-binding domain of the enzymatic colicin E9 is required for toxicity against Escherichia coli cells.

Abstract:

The events that occur after the binding of the enzymatic E colicins to Escherichia coli BtuB receptors that lead to translocation of the cytotoxic domain into the periplasmic space and, ultimately, cell killing are poorly understood. It has been suggested that unfolding of the coiled-coil BtuB receptor binding domain of the E colicins may be an essential step that leads to the loss of immunity protein from the colicin and immunity protein complex and then triggers the events of translocation....

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Authors


Penfold, CN More by this author
Housden, NG More by this author
Boetzel, R More by this author
Vankemmelbeke, M More by this author
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Journal:
Journal of bacteriology
Volume:
186
Issue:
14
Pages:
4520-4527
Publication date:
2004-07-05
DOI:
EISSN:
1098-5530
ISSN:
0021-9193
URN:
uuid:ce5d0087-e42f-4db5-b130-8cbd6812bfa6
Source identifiers:
310231
Local pid:
pubs:310231

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