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

Hecht, O, Zhang, Y, Li, C, Penfold, CN, James, R and Moore, GR (2010) Characterisation of the interaction of colicin A with its co-receptor TolA. FEBS Letters, 584 (11). pp. 2249-52. 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
University of East Anglia > Faculty of Science > Research Groups > Biophysical Chemistry
Depositing User: Deborah Clemitshaw
Date Deposited: 14 Mar 2012 14:55
Last Modified: 25 Jul 2018 04:12
URI: https://ueaeprints.uea.ac.uk/id/eprint/38279
DOI:

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