Structure of AMP-PNP-bound BtuCD and mechanism of ATP-powered vitamin B12 transport by BtuCD-F.
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.
1] Institute of Molecular Biology and Biophysics, Eidgenössische Technische Hochschule Zurich, Zurich, Switzerland. [2] Laboratory of Biomolecular Research, Paul Scherrer Institute, Villigen, Switzerland.
Vladimir M
VM
Korkhov
Institute of Molecular Biology and Biophysics, Eidgenössische Technische Hochschule Zurich, Zurich, Switzerland.
Samantha A
SA
Mireku
Laboratory of Biomolecular Research, Paul Scherrer Institute, Villigen, Switzerland.
Dmitry B
DB
Veprintsev
Institute of Molecular Biology and Biophysics, Eidgenössische Technische Hochschule Zurich, Zurich, Switzerland.
Kaspar P
KP
Locher
D018528:ATP-Binding Cassette Transporters / Q000737:chemistry / Q000378:metabolism*; D000255:Adenosine Triphosphate / Q000378:metabolism*; D000266:Adenylyl Imidodiphosphate / Q000737:chemistry / Q000378:metabolism*; D001692:Biological Transport; D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000737:chemistry / Q000378:metabolism*; D029968:Escherichia coli Proteins / Q000737:chemistry / Q000378:metabolism*; D062105:Molecular Docking Simulation; D033902:Periplasmic Binding Proteins / Q000737:chemistry / Q000378:metabolism*; D011485:Protein Binding; D011487:Protein Conformation; D014805:Vitamin B 12 / Q000378:metabolism*
D018528:ATP-Binding Cassette Transporters; C050021:BtuC peptide, E coli; C050022:BtuD peptide, E coli; D029968:Escherichia coli Proteins; D033902:Periplasmic Binding Proteins; C446048:btuF protein, E coli; D000266:Adenylyl Imidodiphosphate; D000255:Adenosine Triphosphate; D014805:Vitamin B 12