View source for 5zih


==Crystal structure of the red light-activated channelrhodopsin Chrimson.==
<StructureSection load='5zih' size='340' side='right'caption='[[5zih]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5zih]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Chlamydomonas_noctigama Chlamydomonas noctigama] and [https://en.wikipedia.org/wiki/Chlamydomonas_reinhardtii Chlamydomonas reinhardtii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZIH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5ZIH 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]] 2.6&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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=5zih FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5zih OCA], [https://pdbe.org/5zih PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5zih RCSB], [https://www.ebi.ac.uk/pdbsum/5zih PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5zih ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q8L435_CHLRE Q8L435_CHLRE] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Channelrhodopsins are light-activated ion channels that mediate cation permeation across cell membranes upon light absorption. Red-light-activated channelrhodopsins are of particular interest, because red light penetrates deeper into biological tissues and also enables dual-color experiments in combination with blue-light-activated optogenetic tools. Here we report the crystal structure of the most red-shifted channelrhodopsin from the algae Chlamydomonas noctigama, Chrimson, at 2.6 A resolution. Chrimson resembles prokaryotic proton pumps in the retinal binding pocket, while sharing similarity with other channelrhodopsins in the ion-conducting pore. Concomitant mutation analysis identified the structural features that are responsible for Chrimson's red light sensitivity; namely, the protonation of the counterion for the retinal Schiff base, and the polar residue distribution and rigidity of the retinal binding pocket. Based on these mechanistic insights, we engineered ChrimsonSA, a mutant with a maximum activation wavelength red-shifted beyond 605 nm and accelerated closing kinetics.

Crystal structure of the red light-activated channelrhodopsin Chrimson.,Oda K, Vierock J, Oishi S, Rodriguez-Rozada S, Taniguchi R, Yamashita K, Wiegert JS, Nishizawa T, Hegemann P, Nureki O Nat Commun. 2018 Sep 26;9(1):3949. doi: 10.1038/s41467-018-06421-9. PMID:30258177<ref>PMID:30258177</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5zih" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Chlamydomonas noctigama]]
[[Category: Chlamydomonas reinhardtii]]
[[Category: Large Structures]]
[[Category: Hegemann P]]
[[Category: Nishizawa T]]
[[Category: Nureki O]]
[[Category: Oda K]]
[[Category: Oishi S]]
[[Category: Taniguchi R]]
[[Category: Vierock J]]
[[Category: Yamashita K]]