ABC transporter architecture and regulatory roles of accessory domains

Biemans-Oldehinkel, Esther; Doeven, Mark K.; Poolman, Bert

doi:10.1016/j.febslet.2005.11.079

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Volume 580, Issue 4 , Pages 1023-1035, 13 February 2006

ABC transporter architecture and regulatory roles of accessory domains

Edited by Gerrit van Meer

Department of Biochemistry, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Nijenborgh 4, 9747 AG Groningen, The Netherlands

Received 4 November 2005; received in revised form 30 November 2005; accepted 30 November 2005. published online 12 December 2005.

Abstract

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.

Keywords: ABC transporter, Accessory domain, Architecture, ATP-binding cassette, Regulation of transport