期刊
JOURNAL OF BIOENERGETICS AND BIOMEMBRANES
卷 37, 期 6, 页码 475-479出版社
SPRINGER/PLENUM PUBLISHERS
DOI: 10.1007/s10863-005-9494-8
关键词
ABC transporter; NBD; dimerization; MJ0796; MJ1267; catalytic carboxylate; nucleotide binding
资金
- NIGMS NIH HHS [T32GM08203] Funding Source: Medline
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.
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