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4g80
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4g80 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4g80 OCA], [http://pdbe.org/4g80 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4g80 RCSB], [http://www.ebi.ac.uk/pdbsum/4g80 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4g80 ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4g80 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4g80 OCA], [http://pdbe.org/4g80 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4g80 RCSB], [http://www.ebi.ac.uk/pdbsum/4g80 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4g80 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | 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-A displacement along its main axis, accompanied by an ~60 degrees 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. | ||
| + | |||
| + | 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 Nat Struct Mol Biol. 2014 Mar;21(3):244-52. doi: 10.1038/nsmb.2768. Epub 2014 Feb, 2. PMID:24487958<ref>PMID:24487958</ref> | ||
| + | |||
| + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| + | </div> | ||
| + | <div class="pdbe-citations 4g80" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 07:20, 13 December 2017
Crystal structure of voltage sensing domain of Ci-VSP with fragment antibody (WT, 3.8 A)
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