Crystal structure of ATP-binding subunit of an ABC transporter from Geobacillus kaustophilus

Biochem Biophys Res Commun. 2015 Mar 27;459(1):113-7. doi: 10.1016/j.bbrc.2015.02.079. Epub 2015 Feb 25.

Abstract

The ATP binding cassette (ABC) transporters, represent one of the largest superfamilies of primary transporters, which are very essential for various biological functions. The crystal structure of ATP-binding subunit of an ABC transporter from Geobacillus kaustophilus has been determined at 1.77 Å resolution. The crystal structure revealed that the protomer has two thick arms, (arm I and II), which resemble 'L' shape. The ATP-binding pocket is located close to the end of arm I. ATP molecule is docked into the active site of the protein. The dimeric crystal structure of ATP-binding subunit of ABC transporter from G. kaustophilus has been compared with the previously reported crystal structure of ATP-binding subunit of ABC transporter from Salmonella typhimurium.

Keywords: ABC transporter; ATP binding protein; Geobacillus kaustophilus; X-ray diffraction.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • ATP-Binding Cassette Transporters / chemistry*
  • ATP-Binding Cassette Transporters / metabolism*
  • Adenosine Triphosphate / metabolism
  • Amino Acid Sequence
  • Amino Acid Transport Systems, Basic / chemistry
  • Bacterial Proteins / chemistry
  • Bacterial Proteins / metabolism
  • Binding Sites
  • Crystallography, X-Ray
  • Geobacillus / chemistry*
  • Models, Molecular
  • Molecular Docking Simulation
  • Molecular Sequence Data
  • Protein Conformation
  • Protein Multimerization
  • Sequence Alignment

Substances

  • ATP-Binding Cassette Transporters
  • Amino Acid Transport Systems, Basic
  • Bacterial Proteins
  • histidine permease, Bacteria
  • Adenosine Triphosphate

Associated data

  • PDB/4RVC