Published in TB and Outbreaks Week, December 30th, 2003
According to a study from the United States, "cellular import of colicin E3 is initiated by the Escherichia coli outer membrane cobalamin transporter, BtuB. The 135-residue, 100-Angstrom, coiled-coil receptor-binding domain (R135) of colicin E3 forms a 1:1 complex with BtuB, whose structure at a resolution of 2.75 Angstrom is reported.
"Binding of R135 to the BtuB extracellular surface (DeltaG degrees= -12 kcal/mol) is mediated by 27 residues of R135 near the coiled-coil apex. Formation of the R135 BtuB complex results in unfolding of...
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