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==Time-resolved serial femtosecond crystallography reveals early structural changes in channelrhodopsin: 250 microsecond structure==
==Time-resolved serial femtosecond crystallography reveals early structural changes in channelrhodopsin: 250 microsecond structure==
<StructureSection load='7e70' size='340' side='right'caption='[[7e70]]' scene=''>
<StructureSection load='7e70' size='340' side='right'caption='[[7e70]], [[Resolution|resolution]] 2.50&Aring;' 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=7E70 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7E70 FirstGlance]. <br>
<table><tr><td colspan='2'>[[7e70]] 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=7E70 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7E70 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=7e70 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7e70 OCA], [https://pdbe.org/7e70 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7e70 RCSB], [https://www.ebi.ac.uk/pdbsum/7e70 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7e70 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]] 2.5&#8491;</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=7e70 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7e70 OCA], [https://pdbe.org/7e70 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7e70 RCSB], [https://www.ebi.ac.uk/pdbsum/7e70 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7e70 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&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7e70" 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]]

Revision as of 13:06, 6 September 2023

Time-resolved serial femtosecond crystallography reveals early structural changes in channelrhodopsin: 250 microsecond structureTime-resolved serial femtosecond crystallography reveals early structural changes in channelrhodopsin: 250 microsecond structure

Structural highlights

7e70 is a 1 chain structure with sequence from Chlamydomonas reinhardtii. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.5Å
Ligands:, ,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

Q8RUT8_CHLRE Q93WP2_CHLRE

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[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. 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. Time-resolved serial femtosecond crystallography reveals early structural changes in channelrhodopsin. Elife. 2021 Mar 23;10:e62389. PMID:33752801 doi:10.7554/eLife.62389

7e70, resolution 2.50Å

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OCA