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

Nat Struct Mol Biol. 2014 Dec;21(12):1097-9. doi: 10.1038/nsmb.2918. Epub 2014 Nov 17.

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

  • Research Support, Non-U.S. Gov't

MeSH terms

  • ATP-Binding Cassette Transporters / chemistry
  • ATP-Binding Cassette Transporters / metabolism*
  • Adenosine Triphosphate / metabolism*
  • Adenylyl Imidodiphosphate / chemistry
  • Adenylyl Imidodiphosphate / metabolism*
  • Biological Transport
  • Crystallography, X-Ray
  • Escherichia coli / chemistry
  • Escherichia coli / metabolism*
  • Escherichia coli Proteins / chemistry
  • Escherichia coli Proteins / metabolism*
  • Molecular Docking Simulation
  • Periplasmic Binding Proteins / chemistry
  • Periplasmic Binding Proteins / metabolism*
  • Protein Binding
  • Protein Conformation
  • Vitamin B 12 / metabolism*

Substances

  • ATP-Binding Cassette Transporters
  • BtuC peptide, E coli
  • BtuD peptide, E coli
  • Escherichia coli Proteins
  • Periplasmic Binding Proteins
  • btuF protein, E coli
  • Adenylyl Imidodiphosphate
  • Adenosine Triphosphate
  • Vitamin B 12

Associated data

  • PDB/4R9U