ATP hydrolysis induced conformational changes in the vitamin B12 transporter BtuCD revealed by MD simulations
Conformational change of a tryptophan residue in BtuF facilitates binding and transport of cobinamide by the vitamin B12 transporter BtuCD-F
Release of entropic spring reveals conformational coupling mechanism in the ABC transporter BtuCD-F
Single-molecule visualization of conformational changes and substrate transport in the vitamin B12 ABC importer BtuCD-F
Structural basis of nanobody-mediated blocking of BtuF, the cognate substrate-binding protein of the Escherichia coli vitamin B12 transporter BtuCD
Vitamin B12 import is all about timing
Nat. Chem. Biol.
A distinct mechanism for the ABC transporter BtuCD-BtuF revealed by the dynamics of complex formation
Nat. Struct. Mol. Biol.
Asymmetric states of vitamin B12 transporter BtuCD are not discriminated by its cognate substrate binding protein BtuF
Asymmetry in the structure of the ABC transporter-binding protein complex BtuCD-BtuF
Conformational cycle of the vitamin B12 ABC importer in liposomes detected by double electron-electron resonance (DEER)
J. Biol. Chem.