Escherichia Coli

Colicin E3 binds E. coli BtuB, is brought to OmpF for channel transport

Published in TB and Outbreaks Week, December 30th, 2003

Colicin E3 is bound to E. coli BtuB and brought to OmpF on the membrane surface for channel transport.

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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Source: TB and Outbreaks Week (2003-12-30)

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