7c86: Difference between revisions
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<StructureSection load='7c86' size='340' side='right'caption='[[7c86]], [[Resolution|resolution]] 2.30Å' scene=''> | <StructureSection load='7c86' size='340' side='right'caption='[[7c86]], [[Resolution|resolution]] 2.30Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'> | <table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7C86 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7C86 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]] 2.3Å</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]] 2.3Å</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='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=7c86 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7c86 OCA], [https://pdbe.org/7c86 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7c86 RCSB], [https://www.ebi.ac.uk/pdbsum/7c86 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7c86 ProSAT]</span></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=7c86 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7c86 OCA], [https://pdbe.org/7c86 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7c86 RCSB], [https://www.ebi.ac.uk/pdbsum/7c86 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7c86 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Eguma R]] | [[Category: Eguma R]] | ||
Latest revision as of 13:54, 23 October 2024
Time-resolved serial femtosecond crystallography reveals early structural changes in channelrhodopsin: Dark state structureTime-resolved serial femtosecond crystallography reveals early structural changes in channelrhodopsin: Dark state structure
Structural highlights
Publication Abstract from PubMedChannelrhodopsins (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
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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)
OCA- Large Structures
- Eguma R
- Fujiwara T
- Fukuda M
- Hayashi S
- Hegemann P
- Hirata K
- Ikuta T
- Inoue K
- Ishigami I
- Ishitani R
- Ito S
- Iwata S
- Izume T
- Joti Y
- Kandori H
- Kasuya G
- Katayama K
- Kato T
- Kimura T
- Kubo M
- Kusakizako T
- Lee Y
- Maturana AD
- Miyauchi H
- Nakamura R
- Nakane T
- Nango E
- Nishizawa T
- Nomura T
- Nureki O
- Oda K
- Oishi S
- Owada S
- Shihoya W
- Shimada H
- Shimamura T
- Sugahara M
- Takatsuji T
- Takemoto M
- Tanaka R
- Tanaka T
- Taniguchi R
- Tomita A
- Tono K
- Umeda R
- Vierock J
- Yamanaka Y
- Yamashita K