PMID:20433837

Citation	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 Lett. 584:2249-52
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.
Links	PubMed Online version:10.1016/j.febslet.2010.04.061
Keywords	Binding Sites/genetics; Colicins/chemistry; Colicins/genetics; Colicins/metabolism; Epitopes/metabolism; Escherichia coli/metabolism; Escherichia coli Proteins; Peptides/metabolism; Protein Transport/genetics
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