7e71: Difference between revisions
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==Time-resolved serial femtosecond crystallography reveals early structural changes in channelrhodopsin: 1 ms structure== | ==Time-resolved serial femtosecond crystallography reveals early structural changes in channelrhodopsin: 1 ms structure== | ||
<StructureSection load='7e71' size='340' side='right'caption='[[7e71]]' scene=''> | <StructureSection load='7e71' size='340' side='right'caption='[[7e71]], [[Resolution|resolution]] 2.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7E71 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7E71 FirstGlance]. <br> | <table><tr><td colspan='2'>[[7e71]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Chlamydomonas_reinhardtii Chlamydomonas reinhardtii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7E71 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7E71 FirstGlance]. <br> | ||
</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=7e71 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7e71 OCA], [https://pdbe.org/7e71 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7e71 RCSB], [https://www.ebi.ac.uk/pdbsum/7e71 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7e71 ProSAT]</span></td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=OLC:(2R)-2,3-DIHYDROXYPROPYL+(9Z)-OCTADEC-9-ENOATE'>OLC</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=7e71 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7e71 OCA], [https://pdbe.org/7e71 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7e71 RCSB], [https://www.ebi.ac.uk/pdbsum/7e71 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7e71 ProSAT]</span></td></tr> | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/Q8RUT8_CHLRE Q8RUT8_CHLRE] [https://www.uniprot.org/uniprot/Q93WP2_CHLRE Q93WP2_CHLRE] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Channelrhodopsins (ChRs) are microbial light-gated ion channels utilized in optogenetics to control neural activity with light . Light absorption causes retinal chromophore isomerization and subsequent protein conformational changes visualized as optically distinguished intermediates, coupled with channel opening and closing. However, the detailed molecular events underlying channel gating remain unknown. We performed time-resolved serial femtosecond crystallographic analyses of ChR by using an X-ray free electron laser, which revealed conformational changes following photoactivation. The isomerized retinal adopts a twisted conformation and shifts toward the putative internal proton donor residues, consequently inducing an outward shift of TM3, as well as a local deformation in TM7. These early conformational changes in the pore-forming helices should be the triggers that lead to opening of the ion conducting pore. | |||
Time-resolved serial femtosecond crystallography reveals early structural changes in channelrhodopsin.,Oda K, Nomura T, Nakane T, Yamashita K, Inoue K, Ito S, Vierock J, Hirata K, Maturana AD, Katayama K, Ikuta T, Ishigami I, Izume T, Umeda R, Eguma R, Oishi S, Kasuya G, Kato T, Kusakizako T, Shihoya W, Shimada H, Takatsuji T, Takemoto M, Taniguchi R, Tomita A, Nakamura R, Fukuda M, Miyauchi H, Lee Y, Nango E, Tanaka R, Tanaka T, Sugahara M, Kimura T, Shimamura T, Fujiwara T, Yamanaka Y, Owada S, Joti Y, Tono K, Ishitani R, Hayashi S, Kandori H, Hegemann P, Iwata S, Kubo M, Nishizawa T, Nureki O Elife. 2021 Mar 23;10. pii: 62389. doi: 10.7554/eLife.62389. PMID:33752801<ref>PMID:33752801</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 7e71" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Chlamydomonas reinhardtii]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Eguma R]] | [[Category: Eguma R]] | ||