Nucleotide binding domain interactions during the mechanochemical reaction cycle of ATP-binding cassette transporters.
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.
Moody
Jonathan E
JE
Department of Physiology, University of Texas Southwestern Medical Center, 6001 Forest Park Lane, Dallas, Texas 75390-9040, USA.
Thomas
Philip J
PJ
D018528:ATP-Binding Cassette Transporters / Q000737:chemistry* / Q000378:metabolism; D000595:Amino Acid Sequence; D001105:Archaea / Q000737:chemistry; D001665:Binding Sites; D019281:Dimerization; D020409:Molecular Motor Proteins / Q000378:metabolism; D009711:Nucleotides / Q000378:metabolism*
D018528:ATP-Binding Cassette Transporters; D020409:Molecular Motor Proteins; D009711:Nucleotides