Abstract
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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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ATP-Binding Cassette Transporters / chemistry
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ATP-Binding Cassette Transporters / metabolism*
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Adenosine Triphosphate / metabolism*
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Adenylyl Imidodiphosphate / chemistry
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Adenylyl Imidodiphosphate / metabolism*
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Biological Transport
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Crystallography, X-Ray
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Escherichia coli / chemistry
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Escherichia coli / metabolism*
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Escherichia coli Proteins / chemistry
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Escherichia coli Proteins / metabolism*
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Molecular Docking Simulation
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Periplasmic Binding Proteins / chemistry
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Periplasmic Binding Proteins / metabolism*
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Protein Binding
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Protein Conformation
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Vitamin B 12 / metabolism*
Substances
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ATP-Binding Cassette Transporters
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BtuC peptide, E coli
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BtuD peptide, E coli
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Escherichia coli Proteins
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Periplasmic Binding Proteins
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btuF protein, E coli
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Adenylyl Imidodiphosphate
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Adenosine Triphosphate
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Vitamin B 12