4G80
Crystal structure of voltage sensing domain of Ci-VSP with fragment antibody (WT, 3.8 A)
Summary for 4G80
| Entry DOI | 10.2210/pdb4g80/pdb |
| Related | 4G7V 4G7Y |
| Descriptor | Voltage-sensor containing phosphatase, fragment antibody heavy chain, fragment antibody light chain (3 entities in total) |
| Functional Keywords | membrane protein, alpha helix, fragment antibody, voltage sensing domain, sensing voltage |
| Biological source | Ciona intestinalis (sea vase,yellow sea squirt) More |
| Total number of polymer chains | 12 |
| Total formula weight | 258915.78 |
| Authors | |
| Primary citation | Li, Q.,Wanderling, S.,Paduch, M.,Medovoy, D.,Singharoy, A.,McGreevy, R.,Villalba-Galea, C.A.,Hulse, R.E.,Roux, B.,Schulten, K.,Kossiakoff, A.,Perozo, E. Structural mechanism of voltage-dependent gating in an isolated voltage-sensing domain. Nat. Struct. Mol. Biol., 21:244-252, 2014 Cited by PubMed Abstract: 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. PubMed: 24487958DOI: 10.1038/nsmb.2768 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.58 Å) |
Structure validation
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