7AKY

Crystal structure of the viral rhodopsin OLPVR1 in P21212 space group

Summary for 7AKY

• Entry DOI: 10.2210/pdb7aky/pdb
• Descriptor: viral rhodopsin OLPVR1, EICOSANE, (2S)-2,3-dihydroxypropyl (9Z)-hexadec-9-enoate, ... (4 entities in total)
• Functional Keywords: rhodopsin, viral rhodopsin, giant virus, ion channel, retinal, ion transport, light-gated channel, channelrhodopsin, bacteriorhodopsin, membrane protein
• Biological source: Organic Lake phycodnavirus
• Total number of polymer chains: 1
• Total formula weight: 34628.69

Authors

Kovalev, K.,Zabelskii, D.,Alekseev, A.,Astashkin, R.,Gordeliy, V. (deposition date: 2020-10-02, release date: 2020-11-25, Last modification date: 2024-01-31)

Primary citation

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, A.S.,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.
Viral rhodopsins 1 are an unique family of light-gated cation channels.
Nat Commun, 11:5707-5707, 2020

PubMed Abstract: 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 ions. We show that, upon illumination, VirChR1 is able to drive neural firing. The 1.4 Å 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 permeability.

PubMed: 33177509
DOI: 10.1038/s41467-020-19457-7

Experimental method

X-RAY DIFFRACTION (1.4 Å)