Membrane transporters studied by EPR spectroscopy: structure determination and elucidation of functional dynamics

Mullen, Anna, Hall, Jenny, Diegel, Janika, Hassan, Isa, Fey, Adam and MacMillan, Fraser (2016) Membrane transporters studied by EPR spectroscopy: structure determination and elucidation of functional dynamics. Biochemical Society Transactions, 44 (3). pp. 905-915. ISSN 0300-5127

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Abstract

During their mechanistic cycles membrane transporters often undergo extensive conformational changes, sampling a range of orientations, in order to complete their function. Such membrane transporters present somewhat of a challenge to conventional structural studies; indeed, crystallization of membrane-associated proteins sometimes require conditions that vary vastly from their native environments. Moreover, this technique currently only allows for visualization of single selected conformations during any one experiment. EPR spectroscopy is a magnetic resonance technique that offers a unique opportunity to study structural, environmental and dynamic properties of such proteins in their native membrane environments, as well as readily sampling their substrate-binding-induced dynamic conformational changes especially through complementary computational analyses. Here we present a review of recent studies that utilize a variety of EPR techniques in order to investigate both the structure and dynamics of a range of membrane transporters and associated proteins, focusing on both primary (ABC-type transporters) and secondary active transporters which were key interest areas of the late Professor Stephen Baldwin to whom this review is dedicated.

Item Type: Article
Additional Information: The final version of record is available at http://www.biochemsoctrans.org/content/44/3/905
Faculty \ School: Faculty of Science > School of Chemistry
Faculty of Medicine and Health Sciences > Norwich Medical School
Faculty of Science
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Depositing User: Pure Connector
Date Deposited: 24 Sep 2016 00:02
Last Modified: 22 Jul 2020 00:57
URI: https://ueaeprints.uea.ac.uk/id/eprint/59783
DOI: 10.1042/BST20160024

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