The reaction mechanism of BtuCD-F-catalyzed vitamin B12 transport into
Escherichia coli is currently unclear. Here we present the structure of the last
missing state in the form of AMP-PNP-bound BtuCD, trapped by a disulfide
cross-link. Our structural and biochemical data allow a consistent mechanism to
be formulated, thus rationalizing the roles of substrate, ATP and
substrate-binding protein.