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Probing the structure of the mechanosensitive channel of small conductance in lipid bilayers with pulsed electron-electron double resonance

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ward2014biophysj834.pdf (1.948Mb)
Date
18/02/2014
Author
Ward, Richard
Pliotas, Christos
Branigan, Emma
Hacker, Christian
Rasmussen, Akiko
Hagelueken, Gregor
Booth, Ian R
Miller, Samantha
Lucocq, John
Naismith, Jim
Schiemann, Olav
Keywords
QD Chemistry
QH301 Biology
BDC
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Abstract
Mechanosensitive channel proteins are important safety valves against osmotic shock in bacteria, and are involved in sensing touch and sound waves in higher organisms. The mechanosensitive channel of small conductance (MscS) has been extensively studied. Pulsed electron-electron double resonance (PELDOR or DEER) of detergent-solubilized protein confirms that as seen in the crystal structure, the outer ring of transmembrane helices do not pack against the pore- forming helices, creating an apparent void. The relevance of this void to the functional form of MscS in the bilayer is the subject of debate. Here, we report PELDOR measurements of MscS reconstituted into two lipid bilayer systems: nanodiscs and bicelles. The distance measurements from multiple mutants derived from the PELDOR data are consistent with the detergent-solution arrangement of the protein. We conclude, therefore, that the relative positioning of the transmembrane helices is preserved in mimics of the cell bilayer, and that the apparent voids are not an artifact of detergent solution but a property of the protein that will have to be accounted for in any molecular mechanism of gating.
Citation
Ward , R , Pliotas , C , Branigan , E , Hacker , C , Rasmussen , A , Hagelueken , G , Booth , I R , Miller , S , Lucocq , J , Naismith , J & Schiemann , O 2014 , ' Probing the structure of the mechanosensitive channel of small conductance in lipid bilayers with pulsed electron-electron double resonance ' , Biophysical Journal , vol. 106 , no. 4 , pp. 834-842 . https://doi.org/10.1016/j.bpj.2014.01.008
Publication
Biophysical Journal
Status
Peer reviewed
DOI
https://doi.org/10.1016/j.bpj.2014.01.008
ISSN
0006-3495
Type
Journal article
Rights
Copyright © 2014 The Authors. This is an Open Access article distributed under the terms of the Creative Commons-Attribution Noncommercial License (http://creativecommons.org/licenses/by-nc/2.0/), which permits unrestricted noncommercial use, distribution, and reproduction in any medium, provided the original work is properly cited.
Description
Funding: EaStCHEM studentship to E.B. The work was funded by BBSRC grant BB/H017917/1 to JNH, OS & IRB, The Leverhulme Foundation (EM-2012-60\2) and equipment from a Wellcome Trust Capital Award.
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  • University of St Andrews Research
URL
http://www.ncbi.nlm.nih.gov/pubmed/24559986
URI
http://hdl.handle.net/10023/4780

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