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

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

Author information

1
Department of Biochemistry, The Bruce and Ruth Rappaport Faculty of Medicine, The Technion-Israel Institute of Technology, 31096 Haifa, Israel. Electronic address: lewinson@tx.technion.ac.il.
2
Department of Biochemistry, The Bruce and Ruth Rappaport Faculty of Medicine, The Technion-Israel Institute of Technology, 31096 Haifa, Israel.

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

PMID:
28104364
DOI:
10.1016/j.jmb.2017.01.010
[Indexed for MEDLINE]
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