View source for 6eig


==Crystal structure of N24Q/C128T mutant of Channelrhodopsin 2==
<StructureSection load='6eig' size='340' side='right'caption='[[6eig]], [[Resolution|resolution]] 2.70&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6eig]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6EIG OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6EIG FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=LFA:EICOSANE'>LFA</scene>, <scene name='pdbligand=OLC:(2R)-2,3-DIHYDROXYPROPYL+(9Z)-OCTADEC-9-ENOATE'>OLC</scene>, <scene name='pdbligand=PO4:PHOSPHATE+ION'>PO4</scene></td></tr>
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=LYR:N~6~-[(2Z,4E,6E,8E)-3,7-DIMETHYL-9-(2,6,6-TRIMETHYLCYCLOHEX-1-EN-1-YL)NONA-2,4,6,8-TETRAENYL]LYSINE'>LYR</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6eig FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6eig OCA], [http://pdbe.org/6eig PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6eig RCSB], [http://www.ebi.ac.uk/pdbsum/6eig PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6eig ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The light-gated ion channel channelrhodopsin 2 (ChR2) from Chlamydomonas reinhardtii is a major optogenetic tool. Photon absorption starts a well-characterized photocycle, but the structural basis for the regulation of channel opening remains unclear. We present high-resolution structures of ChR2 and the C128T mutant, which has a markedly increased open-state lifetime. The structure reveals two cavities on the intracellular side and two cavities on the extracellular side. They are connected by extended hydrogen-bonding networks involving water molecules and side-chain residues. Central is the retinal Schiff base that controls and synchronizes three gates that separate the cavities. Separate from this network is the DC gate that comprises a water-mediated bond between C128 and D156 and interacts directly with the retinal Schiff base. Comparison with the C128T structure reveals a direct connection of the DC gate to the central gate and suggests how the gating mechanism is affected by subtle tuning of the Schiff base's interactions.

Structural insights into ion conduction by channelrhodopsin 2.,Volkov O, Kovalev K, Polovinkin V, Borshchevskiy V, Bamann C, Astashkin R, Marin E, Popov A, Balandin T, Willbold D, Buldt G, Bamberg E, Gordeliy V Science. 2017 Nov 24;358(6366). pii: 358/6366/eaan8862. doi:, 10.1126/science.aan8862. PMID:29170206<ref>PMID:29170206</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6eig" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Astashkin, R]]
[[Category: Balandin, T]]
[[Category: Bamann, C]]
[[Category: Bamberg, E]]
[[Category: Borshchevskiy, V]]
[[Category: Bueldt, G]]
[[Category: Gordeliy, V]]
[[Category: Kovalev, K]]
[[Category: Marin, E]]
[[Category: Polovinkin, V]]
[[Category: Popov, A]]
[[Category: Volkov, O]]
[[Category: Willlbold, D]]
[[Category: Ion transport]]
[[Category: Membrane protein]]
[[Category: Retinal protein]]