Nucleotide binding domain interactions during the mechanochemical reaction cycle of ATP-binding cassette transporters

Jonathan E. Moody, Philip J. Thomas

Research output: Contribution to journalArticle

26 Citations (Scopus)

Abstract

ATP-binding cassette (ABC) transporters serve as importers and exporters for a wide variety of solutes in both prokaryotes and eukaryotes, and are implicated in microbial drug resistance and a number of significant human genetic disorders. Initial crystal structures of the soluble nucleotide binding domains (NBDs) of ABC transporters, while a significant step towards understanding the coupling of ATP binding and hydrolysis to transport, presented researchers with important questions surrounding the role of the signature sequence residues, the composition of the nucleotide binding sites, and the mode of NBD dimerization during the transport reaction cycle. Recent studies have begun to address these concerns. This mini-review summarizes the biochemical and structural characterizations of two archaebacterial NBDs from Methanocaldococcus jannaschii, MJ0796 and MJ1267, and offers current perspectives on the functional mechanism of ABC transporters.

Original languageEnglish (US)
Pages (from-to)475-479
Number of pages5
JournalJournal of Bioenergetics and Biomembranes
Volume37
Issue number6
DOIs
StatePublished - Dec 2005

Fingerprint

ATP-Binding Cassette Transporters
Nucleotides
Methanocaldococcus
Inborn Genetic Diseases
Medical Genetics
Dimerization
Microbial Drug Resistance
Eukaryota
Hydrolysis
Adenosine Triphosphate
Binding Sites
Research Personnel

Keywords

  • ABC transporter
  • Catalytic carboxylate
  • Dimerization
  • MJ0796
  • MJ1267
  • NBD
  • Nucleotide binding

ASJC Scopus subject areas

  • Physiology
  • Cell Biology

Cite this

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