Characterisation of the interaction of colicin A with its co-receptor TolA

Hecht, Oliver, Zhang, Ying, Li, Chan, Penfold, Christopher N., James, Richard and Moore, Geoffrey R. (2010) Characterisation of the interaction of colicin A with its co-receptor TolA. FEBS Letters, 584 (11). pp. 2249-2252. ISSN 0014-5793

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Abstract

Colicin A enters Escherichia coli cells through interaction with endogenous TolA and TolB proteins. In vitro, binding of the colicin A translocation domain to TolA leads to unfolding of TolA. Through NMR studies of the colicin A translocation domain and polypeptides representing the individual TolA and TolB binding epitopes of colicin A we question if the unfolding of TolA induced by colicin A is likely to be physiologically relevant. The NMR data further reveals that the colicin A binding site on TolA is different from that for colicin N which explains why there is a difference in colicin toxicity for E. coli carrying a TolA-III homologue from Yersina enterocolitica in place of its own TolA-III.

Item Type: Article
Faculty \ School: Faculty of Science > School of Chemistry
Depositing User: Users 2731 not found.
Date Deposited: 14 Mar 2012 14:55
Last Modified: 21 Apr 2020 17:01
URI: https://ueaeprints.uea.ac.uk/id/eprint/38279
DOI: 10.1016/j.febslet.2010.04.061

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