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The structure of BtuB with bound colicin E3 R-domain implies a translocon
Nature Structural & Molecular Biology
Cellular import of colicin E3 is initiated by the Escherichia coli outer membrane cobalamin transporter, BtuB. The 135-residue 100-Å coiled-coil receptor-binding domain (R135) of colicin E3 forms a 1:1 complex with BtuB whose structure at a resolution of 2.75 Å is reported. Binding of R135 to the BtuB extracellular surface (∆G°= -12 kcal mol -1 ) is mediated by 27 residues of R135 near the coiled-coil apex. Formation of the R135-BtuB complex results in unfolding of R135 N-and C-terminal ends,doi:10.1038/nsb997 pmid:14528295 fatcat:omzaytdq2nakjg5qultsc4dtey