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XB-ART-48918
Nat Struct Mol Biol 2014 Mar 01;213:244-52. doi: 10.1038/nsmb.2768.
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Structural mechanism of voltage-dependent gating in an isolated voltage-sensing domain.

Li Q , Wanderling S , Paduch M , Medovoy D , Singharoy A , McGreevy R , Villalba-Galea CA , Hulse RE , Roux B , Schulten K , Kossiakoff A , Perozo E .


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The transduction of transmembrane electric fields into protein motion has an essential role in the generation and propagation of cellular signals. Voltage-sensing domains (VSDs) carry out these functions through reorientations of positive charges in the S4 helix. Here, we determined crystal structures of the Ciona intestinalis VSD (Ci-VSD) in putatively active and resting conformations. S4 undergoes an ~5-Å displacement along its main axis, accompanied by an ~60° rotation. This movement is stabilized by an exchange in countercharge partners in helices S1 and S3 that generates an estimated net charge transfer of ~1 eo. Gating charges move relative to a ''hydrophobic gasket' that electrically divides intra- and extracellular compartments. EPR spectroscopy confirms the limited nature of S4 movement in a membrane environment. These results provide an explicit mechanism for voltage sensing and set the basis for electromechanical coupling in voltage-dependent enzymes and ion channels.

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References [+] :
Adams, PHENIX: a comprehensive Python-based system for macromolecular structure solution. 2010, Pubmed