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Literature summary for 7.6.2.8 extracted from

  • Joseph, B.; Jeschke, G.; Goetz, B.A.; Locher, K.P.; Bordignon, E.
    Transmembrane gate movements in the type II ATP-binding cassette (ABC) importer BtuCD-F during nucleotide cycle (2011), J. Biol. Chem., 286, 41008-41017.
    View publication on PubMedView publication on EuropePMC
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Crystallization (Commentary)

Crystallization (Comment) Organism
elucidation of gating mechanism by EPR spectroscopy. The translocation gates of the BtuCDF complex undergo conformational changes in line with a two-state alternating access model. Binding of ATP drives the gates to an inward-facing conformation. Following ATP hydrolysis, the translocation gates restore to an apo-like conformation. In the presence of ATP, an excess of vitamin B12 promotes the reopening of the gates toward the periplasm and the dislodgement of BtuF from the transporter Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli P06609 permease protein BtuC
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Reaction

Reaction Comment Organism Reaction ID
ATP + H2O + vitamin B12-[cobalamin-binding protein][side 1] = ADP + phosphate + vitamin B12[side 2] + [cobalamin-binding protein][side 1] the translocation gates of the BtuCDF complex undergo conformational changes in line with a two-state alternating access model. Binding of ATP drives the gates to an inward-facing conformation. Following ATP hydrolysis, the translocation gates restore to an apo-like conformation. In the presence of ATP, an excess of vitamin B12 promotes the reopening of the gates toward the periplasm and the dislodgement of BtuF from the transporter Escherichia coli
a