Characterisation of the interaction of colicin A with its co-receptor TolA.
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.
Hecht
Oliver
O
Centre for Molecular and Structural Biochemistry, School of Chemical Sciences, University of East Anglia, Norwich, UK.
Zhang
Ying
Y
Li
Chan
C
Penfold
Christopher N
CN
James
Richard
R
Moore
Geoffrey R
GR
D001665:Binding Sites / Q000235:genetics; D003087:Colicins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism*; D000939:Epitopes / Q000378:metabolism*; D004926:Escherichia coli / Q000378:metabolism*; D029968:Escherichia coli Proteins; D010455:Peptides / Q000378:metabolism*; D021381:Protein Transport / Q000235:genetics
D003087:Colicins; D000939:Epitopes; D029968:Escherichia coli Proteins; D010455:Peptides