View source for 6edq


==Crystal Structure of the Light-Gated Anion Channelrhodopsin GtACR1==
<StructureSection load='6edq' size='340' side='right'caption='[[6edq]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6edq]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Guillardia_theta_CCMP2712 Guillardia theta CCMP2712]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6EDQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6EDQ FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.9&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <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>, <scene name='pdbligand=OLC:(2R)-2,3-DIHYDROXYPROPYL+(9Z)-OCTADEC-9-ENOATE'>OLC</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6edq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6edq OCA], [https://pdbe.org/6edq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6edq RCSB], [https://www.ebi.ac.uk/pdbsum/6edq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6edq ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/L1J207_GUITC L1J207_GUITC] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The anion channelrhodopsin GtACR1 from the alga Guillardia theta is a potent neuron-inhibiting optogenetics tool. Presented here, its X-ray structure at 2.9 A reveals a tunnel traversing the protein from its extracellular surface to a large cytoplasmic cavity. The tunnel is lined primarily by small polar and aliphatic residues essential for anion conductance. A disulfide-immobilized extracellular cap facilitates channel closing and the ion path is blocked mid-membrane by its photoactive retinylidene chromophore and further by a cytoplasmic side constriction. The structure also reveals a novel photoactive site configuration that maintains the retinylidene Schiff base protonated when the channel is open. These findings suggest a new channelrhodopsin mechanism, in which the Schiff base not only controls gating, but also serves as a direct mediator for anion flux.

Crystal structure of a natural light-gated anion channelrhodopsin.,Li H, Huang CY, Govorunova EG, Schafer CT, Sineshchekov OA, Wang M, Zheng L, Spudich JL Elife. 2019 Jan 7;8. pii: 41741. doi: 10.7554/eLife.41741. PMID:30614787<ref>PMID:30614787</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6edq" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Guillardia theta CCMP2712]]
[[Category: Large Structures]]
[[Category: Huang CY]]
[[Category: Li H]]
[[Category: Spudich JL]]
[[Category: Wang M]]
[[Category: Zheng L]]