View source for 9cde


==Kalium channelrhodopsin 1 C110A mutant from Hyphochytrium catenoides, Continuous Illumination State==
<StructureSection load='9cde' size='340' side='right'caption='[[9cde]], [[Resolution|resolution]] 3.44&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9cde]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Hyphochytrium_catenoides Hyphochytrium catenoides]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9CDE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9CDE FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.44&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CLR:CHOLESTEROL'>CLR</scene>, <scene name='pdbligand=PEE:1,2-DIOLEOYL-SN-GLYCERO-3-PHOSPHOETHANOLAMINE'>PEE</scene>, <scene name='pdbligand=RET:RETINAL'>RET</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=9cde FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9cde OCA], [https://pdbe.org/9cde PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9cde RCSB], [https://www.ebi.ac.uk/pdbsum/9cde PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9cde ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Structural information on channelrhodopsins' mechanism of light-gated ion conductance is scarce, limiting its engineering as optogenetic tools. Here, we use single-particle cryo-electron microscopy of peptidisc-incorporated protein samples to determine the structures of the slow-cycling mutant C110A of kalium channelrhodopsin 1 from Hyphochytrium catenoides (HcKCR1) in the dark and upon laser flash excitation. Upon photoisomerization of the retinal chromophore, the retinylidene Schiff base NH-bond reorients from the extracellular to the cytoplasmic side. This switch triggers a series of side chain reorientations and merges intramolecular cavities into a transmembrane K(+) conduction pathway. Molecular dynamics simulations confirm K(+) flux through the illuminated state but not through the resting state. The overall displacement between the closed and the open structure is small, involving mainly side chain rearrangements. Asp105 and Asp116 play a key role in K(+) conductance. Structure-guided mutagenesis and patch-clamp analysis reveal the roles of the pathway-forming residues in channel gating and selectivity.

Structural insights into light-gating of potassium-selective channelrhodopsin.,Morizumi T, Kim K, Li H, Nag P, Dogon T, Sineshchekov OA, Wang Y, Brown LS, Hwang S, Sun H, Bondar AN, Schapiro I, Govorunova EG, Spudich JL, Ernst OP Nat Commun. 2025 Feb 3;16(1):1283. doi: 10.1038/s41467-025-56491-9. PMID:39900567<ref>PMID:39900567</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 9cde" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Hyphochytrium catenoides]]
[[Category: Large Structures]]
[[Category: Ernst OP]]
[[Category: Kim K]]
[[Category: Morizumi T]]