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ABC transporter architecture and regulatory roles of accessory domains
Author(s) -
Biemans-Oldehinkel Esther,
Doeven Mark K.,
Poolman Bert
Publication year - 2006
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2005.11.079
Subject(s) - atp binding cassette transporter , function (biology) , transporter , cyclic nucleotide binding domain , biology , computational biology , nucleotide , microbiology and biotechnology , biochemistry , gene
We present an overview of the architecture of ATP‐binding cassette (ABC) transporters and dissect the systems in core and accessory domains. The ABC transporter core is formed by the transmembrane domains (TMDs) and the nucleotide binding domains (NBDs) that constitute the actual translocator. The accessory domains include the substrate‐binding proteins, that function as high affinity receptors in ABC type uptake systems, and regulatory or catalytic domains that can be fused to either the TMDs or NBDs. The regulatory domains add unique functions to the transporters allowing the systems to act as channel conductance regulators, osmosensors/regulators, and assemble into macromolecular complexes with specific properties.