The Voltage-Dependent Deactivation of the KvAP Channel Involves the Breakage of Its S4 Helix

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serval:BIB_9F3F3B036C88
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Article: article from journal or magazin.
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Title
The Voltage-Dependent Deactivation of the KvAP Channel Involves the Breakage of Its S4 Helix
Journal
Frontiers in Molecular Biosciences
Author(s)
Bignucolo Olivier, Bernèche Simon
ISSN
2296-889X
Publication state
In Press
Language
english
Abstract
We show that the response of the KvAP voltage-sensor domain to membrane polarization consists in two co-occurring conformational changes: the rupture of the Asp62-Arg133 salt-bridge and the breakage of the S4 helix. This finding is consistent with the hypothesis that the breakage of S4 is a general feature of non-swapped Kv channels. Upon polarization, the N-ter segment of the S4 helix translates toward the intracellular side of the membrane, which allows to solve previously paradoxical avidin accessibility measurements. Simulations involving the recently solved whole structure of KvAP show how these conformational changes induce a reorientation of the S5 and pore helices, putatively leading to the constriction and closure of the selectivity filter. This study also links mechanistic insights in prokaryotic potassium channel membrane potential sensing with the perspective of finding new antibiotic targets.
Create date
03/08/2020 11:46
Last modification date
10/09/2020 5:22
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