منابع مشابه
Abc Transporters in Mitochondria
Mitochondria are essential organelles of most eukaryotic cells including fungi, invertebrates, vertebrates and plants. They perform various processes such as oxidative phosphorylation, the tricarboxylic acid cycle, fatty acid oxidation, the biosynthesis of various amino acids, the generation of iron-sulfur (Fe/S) clusters and their insertion into apoproteins, as well as partial reactions of hem...
متن کاملStructure of ABC transporters.
ABC (ATP-binding cassette) transporters are primary active membrane proteins that translocate solutes (allocrites) across lipid bilayers. The prototypical ABC transporter consists of four domains: two cytoplasmic NBDs (nucleotide-binding domains) and two TMDs (transmembrane domains). The NBDs, whose primary sequence is highly conserved throughout the superfamily, bind and hydrolyse ATP to power...
متن کاملPeroxisomal ABC transporters.
The set of proteins found in the membranes of mammalian peroxisomes includes four half ABC transporters (ALDP, ALDR, PMP70, P70R) comprising a distinct subset of the superfamily of ABC transporters designated subfamily D. Each has an N-terminal hydrophobic transmembrane domain with multiple transmembrane segments (TMS) and a hydrophilic C-terminal half containing a nucleotide-binding domain (NB...
متن کاملABC transporters: bacterial exporters.
The ABC transporters (also called traffic ATPases) make up a large superfamily of proteins which share a common function and a common ATP-binding domain. ABC transporters are classified into three major groups: bacterial importers (the periplasmic permeases), eukaryotic transporters, and bacterial exporters. We present a comprehensive review of the bacterial ABC exporter group, which currently ...
متن کاملStructural diversity of ABC transporters
ATP-binding cassette (ABC) transporters form a large superfamily of ATP-dependent protein complexes that mediate transport of a vast array of substrates across membranes. The 14 currently available structures of ABC transporters have greatly advanced insight into the transport mechanism and revealed a tremendous structural diversity. Whereas the domains that hydrolyze ATP are structurally relat...
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ژورنال
عنوان ژورنال: FEBS Letters
سال: 2006
ISSN: 0014-5793
DOI: 10.1016/j.febslet.2006.01.015