Snapshots of the maltose transporter during ATP hydrolysis

Proc Natl Acad Sci U S A. 2011 Sep 13;108(37):15152-6. doi: 10.1073/pnas.1108858108. Epub 2011 Aug 8.

Abstract

ATP-binding cassette transporters are powered by ATP, but the mechanism by which these transporters hydrolyze ATP is unclear. In this study, four crystal structures of the full-length wild-type maltose transporter, stabilized by adenosine 5'-(β,γ-imido)triphosphate or ADP in conjunction with phosphate analogs BeF(3)(-), VO(4)(3-), or AIF(4)(-), were determined to 2.2- to 2.4-Å resolution. These structures led to the assignment of two enzymatic states during ATP hydrolysis and demonstrate specific functional roles of highly conserved residues in the nucleotide-binding domain, suggesting that ATP-binding cassette transporters catalyze ATP hydrolysis via a general base mechanism.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenosine Triphosphate / metabolism*
  • Adenylyl Imidodiphosphate / metabolism
  • Biocatalysis
  • Catalytic Domain
  • Escherichia coli Proteins / chemistry
  • Escherichia coli Proteins / metabolism*
  • Hydrolysis
  • Maltose / metabolism*
  • Maltose-Binding Proteins / metabolism
  • Models, Molecular
  • Mutant Proteins / chemistry
  • Mutant Proteins / metabolism
  • Protein Structure, Secondary

Substances

  • Escherichia coli Proteins
  • Maltose-Binding Proteins
  • Mutant Proteins
  • Adenylyl Imidodiphosphate
  • Maltose
  • Adenosine Triphosphate

Associated data

  • PDB/3PUV
  • PDB/3PUW
  • PDB/3PUX
  • PDB/3RLF