Journal
JOURNAL OF BIOENERGETICS AND BIOMEMBRANES
Volume 37, Issue 6, Pages 475-479Publisher
SPRINGER/PLENUM PUBLISHERS
DOI: 10.1007/s10863-005-9494-8
Keywords
ABC transporter; NBD; dimerization; MJ0796; MJ1267; catalytic carboxylate; nucleotide binding
Categories
Funding
- NIGMS NIH HHS [T32GM08203] Funding Source: Medline
Ask authors/readers for more resources
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 oil the functional mechanism of ABC transporters.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available