7aky: Difference between revisions
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==Crystal structure of the viral rhodopsin OLPVR1 in P21212 space group== | |||
<StructureSection load='7aky' size='340' side='right'caption='[[7aky]], [[Resolution|resolution]] 1.40Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[7aky]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Organic_Lake_phycodnavirus Organic Lake phycodnavirus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7AKY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7AKY 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]] 1.4Å</td></tr> | |||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=97N:(2S)-2,3-DIHYDROXYPROPYL+(9Z)-HEXADEC-9-ENOATE'>97N</scene>, <scene name='pdbligand=LFA:EICOSANE'>LFA</scene>, <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></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=7aky FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7aky OCA], [https://pdbe.org/7aky PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7aky RCSB], [https://www.ebi.ac.uk/pdbsum/7aky PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7aky ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/F2Y337_9PHYC F2Y337_9PHYC] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Phytoplankton is the base of the marine food chain as well as oxygen and carbon cycles and thus plays a global role in climate and ecology. Nucleocytoplasmic Large DNA Viruses that infect phytoplankton organisms and regulate the phytoplankton dynamics encompass genes of rhodopsins of two distinct families. Here, we present a functional and structural characterization of two proteins of viral rhodopsin group 1, OLPVR1 and VirChR1. Functional analysis of VirChR1 shows that it is a highly selective, Na(+)/K(+)-conducting channel and, in contrast to known cation channelrhodopsins, it is impermeable to Ca(2+) ions. We show that, upon illumination, VirChR1 is able to drive neural firing. The 1.4 A resolution structure of OLPVR1 reveals remarkable differences from the known channelrhodopsins and a unique ion-conducting pathway. Thus, viral rhodopsins 1 represent a unique, large group of light-gated channels (viral channelrhodopsins, VirChR1s). In nature, VirChR1s likely mediate phototaxis of algae enhancing the host anabolic processes to support virus reproduction, and therefore, might play a major role in global phytoplankton dynamics. Moreover, VirChR1s have unique potential for optogenetics as they lack possibly noxious Ca(2+) permeability. | |||
Viral rhodopsins 1 are an unique family of light-gated cation channels.,Zabelskii D, Alekseev A, Kovalev K, Rankovic V, Balandin T, Soloviov D, Bratanov D, Savelyeva E, Podolyak E, Volkov D, Vaganova S, Astashkin R, Chizhov I, Yutin N, Rulev M, Popov A, Eria-Oliveira AS, Rokitskaya T, Mager T, Antonenko Y, Rosselli R, Armeev G, Shaitan K, Vivaudou M, Buldt G, Rogachev A, Rodriguez-Valera F, Kirpichnikov M, Moser T, Offenhausser A, Willbold D, Koonin E, Bamberg E, Gordeliy V Nat Commun. 2020 Nov 11;11(1):5707. doi: 10.1038/s41467-020-19457-7. PMID:33177509<ref>PMID:33177509</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 7aky" style="background-color:#fffaf0;"></div> | ||
[[Category: Astashkin | |||
[[Category: Gordeliy | ==See Also== | ||
[[Category: | *[[Rhodopsin 3D structures|Rhodopsin 3D structures]] | ||
[[Category: Zabelskii | == References == | ||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Organic Lake phycodnavirus]] | |||
[[Category: Alekseev A]] | |||
[[Category: Astashkin R]] | |||
[[Category: Gordeliy V]] | |||
[[Category: Kovalev K]] | |||
[[Category: Zabelskii D]] | |||
Latest revision as of 15:11, 1 February 2024
Crystal structure of the viral rhodopsin OLPVR1 in P21212 space groupCrystal structure of the viral rhodopsin OLPVR1 in P21212 space group
Structural highlights
FunctionPublication Abstract from PubMedPhytoplankton is the base of the marine food chain as well as oxygen and carbon cycles and thus plays a global role in climate and ecology. Nucleocytoplasmic Large DNA Viruses that infect phytoplankton organisms and regulate the phytoplankton dynamics encompass genes of rhodopsins of two distinct families. Here, we present a functional and structural characterization of two proteins of viral rhodopsin group 1, OLPVR1 and VirChR1. Functional analysis of VirChR1 shows that it is a highly selective, Na(+)/K(+)-conducting channel and, in contrast to known cation channelrhodopsins, it is impermeable to Ca(2+) ions. We show that, upon illumination, VirChR1 is able to drive neural firing. The 1.4 A resolution structure of OLPVR1 reveals remarkable differences from the known channelrhodopsins and a unique ion-conducting pathway. Thus, viral rhodopsins 1 represent a unique, large group of light-gated channels (viral channelrhodopsins, VirChR1s). In nature, VirChR1s likely mediate phototaxis of algae enhancing the host anabolic processes to support virus reproduction, and therefore, might play a major role in global phytoplankton dynamics. Moreover, VirChR1s have unique potential for optogenetics as they lack possibly noxious Ca(2+) permeability. Viral rhodopsins 1 are an unique family of light-gated cation channels.,Zabelskii D, Alekseev A, Kovalev K, Rankovic V, Balandin T, Soloviov D, Bratanov D, Savelyeva E, Podolyak E, Volkov D, Vaganova S, Astashkin R, Chizhov I, Yutin N, Rulev M, Popov A, Eria-Oliveira AS, Rokitskaya T, Mager T, Antonenko Y, Rosselli R, Armeev G, Shaitan K, Vivaudou M, Buldt G, Rogachev A, Rodriguez-Valera F, Kirpichnikov M, Moser T, Offenhausser A, Willbold D, Koonin E, Bamberg E, Gordeliy V Nat Commun. 2020 Nov 11;11(1):5707. doi: 10.1038/s41467-020-19457-7. PMID:33177509[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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