Structure of AMP-PNP-bound BtuCD and mechanism of ATP-powered vitamin B12 transport by BtuCD-F

• Published in: Nature structural & molecular biology Vol. 21; no. 12; pp. 1097 - 1099
• Main Authors: Korkhov, Vladimir M, Mireku, Samantha A, Veprintsev, Dmitry B, Locher, Kaspar P
• Format: Journal Article
• Language: English
• Published: United States Nature Publishing Group 01.12.2014
• Subjects: Adenosine Triphosphate - metabolism; Adenylyl Imidodiphosphate - chemistry; Adenylyl Imidodiphosphate - metabolism; ATP-Binding Cassette Transporters - chemistry; ATP-Binding Cassette Transporters - metabolism; Biochemistry; Biological Transport; Crosslinking; Crystallization; Crystallography, X-Ray; E coli; Escherichia coli; Escherichia coli - chemistry; Escherichia coli - metabolism; Escherichia coli Proteins - chemistry; Escherichia coli Proteins - metabolism; Molecular Docking Simulation; Molecular structure; Periplasmic Binding Proteins - chemistry; Periplasmic Binding Proteins - metabolism; Physiological aspects; Protein Binding; Protein Conformation; Proteins; Vitamin B 12 - metabolism; Vitamin B12
• ISSN: 1545-9993; 1545-9985
• DOI: 10.1038/nsmb.2918

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.