Mechanism of Action of ABC Importers: Conservation, Divergence, and Physiological Adaptations

Oded Lewinson; Nurit Livnat-Levanon

doi:10.1016/j.jmb.2017.01.010

Mechanism of Action of ABC Importers: Conservation, Divergence, and Physiological Adaptations

J Mol Biol. 2017 Mar 10;429(5):606-619. doi: 10.1016/j.jmb.2017.01.010. Epub 2017 Jan 16.

Authors

Oded Lewinson¹, Nurit Livnat-Levanon²

Affiliations

¹ Department of Biochemistry, The Bruce and Ruth Rappaport Faculty of Medicine, The Technion-Israel Institute of Technology, 31096 Haifa, Israel. Electronic address: [email protected].
² Department of Biochemistry, The Bruce and Ruth Rappaport Faculty of Medicine, The Technion-Israel Institute of Technology, 31096 Haifa, Israel.

PMID: 28104364
DOI: 10.1016/j.jmb.2017.01.010

Abstract

The past decade has seen a remarkable surge in structural characterization of ATP binding cassette (ABC) transporters, which have spurred a more focused functional analysis of these elaborate molecular machines. As a result, it has become increasingly apparent that there is a substantial degree of mechanistic variation between ABC transporters that function as importers, which correlates with their physiological roles. Here, we summarize recent advances in ABC importers' structure-function studies and provide an explanation as to the origin of the different mechanisms of action.

Keywords: ABC transporter; ATP hydrolysis; membrane protein; structure–function; substrate-binding protein.

Publication types

Review
Research Support, Non-U.S. Gov't

MeSH terms

ATP-Binding Cassette Transporters / genetics
ATP-Binding Cassette Transporters / metabolism*
Adaptation, Physiological
Adenosine Triphosphate / genetics
Adenosine Triphosphate / metabolism
Models, Molecular
Protein Conformation

Substances

ATP-Binding Cassette Transporters
Adenosine Triphosphate