Viral rhodopsins 1 are an unique family of light-gated cation channels.

Animals Calcium / metabolism Cations Cells, Cultured Channelrhodopsins / metabolism HEK293 Cells Humans Ion Channel Gating Light Neurons / metabolism Phylogeny Phytoplankton / virology Protein Conformation Rats, Wistar Rhodopsin / chemistry Structure-Activity Relationship Viral Proteins / chemistry X-Ray Diffraction

Journal

Nature communications

ISSN: 2041-1723

Titre abrégé: Nat Commun

Pays: England

ID NLM: 101528555

Informations de publication

Date de publication:
11 11 2020

Historique:

received: 22 07 2020

accepted: 07 10 2020

entrez: 12 11 2020

pubmed: 13 11 2020

medline: 15 12 2020

Statut: epublish

Résumé

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

Identifiants

DOI: 10.1038/s41467-020-19457-7 PMID: 33177509 PMC: PMC7659345

pubmed: 33177509

doi: 10.1038/s41467-020-19457-7

pii: 10.1038/s41467-020-19457-7

pmc: PMC7659345

doi:

Substances chimiques

Cations 0

Channelrhodopsins 0

Viral Proteins 0

Rhodopsin 9009-81-8

Calcium SY7Q814VUP

Types de publication

Journal Article Research Support, Non-U.S. Gov't

Langues

eng

Sous-ensembles de citation

Pagination

5707

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