Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 117, Issue 8, Pages 4131-4141Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1915888117
Keywords
rhodopsin; membrane protein; X-ray crystallography; crystal structure; retinal
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Funding
- common program of Agence Nationale de la Recherche (ANR), France
- Deutsche Forschungsgemeinschaft, Germany [ANR-15-CE11-0029-02/FA 301/11-1, MA 7525/1-1]
- Frankfurt: Cluster of Excellence Frankfurt Macromolecular Complexes by the Max Planck Society
- Commissariat a l'EnergieAtomique et aux Energies Alternatives (Institut de Biologie Structurale)-Helmholtz-Gemeinschaft Deutscher Forschungszentren (Forschungszentrum Julich) Special Terms and Conditions 5.1 Specific Agreement
- French Infrastructure for Integrated Structural Biology (FRISBI) [ANR-10-INBS-05-02]
- Grenoble Alliance for Integrated Structural Cell Biology (GRAL), a project of University Grenoble Alpes Graduate School (Ecoles Universitaires de Recherche) CBH-EUR-GS Grant [ANR-17-EURE-0003]
- Russian Foundation for Basic Research (RFBR)
- CNRS [19-52-15017]
- RFBR [18-04-00503a]
- Russian Science Foundation (RSF) [19-44-06302]
- L'Application des Epreuves Individuelles/The Spanish Federation of Rare Diseases (AEI/FEDER), European Union (EU) ['VIREVO' CGL2016-76273-P]
- FEDER funds
- Russian Science Foundation [19-44-06302] Funding Source: Russian Science Foundation
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Rhodopsins are the most abundant light-harvesting proteins. A new family of rhodopsins, heliorhodopsins (HeRs), has recently been discovered. Unlike in the known rhodopsins, in HeRs the N termini face the cytoplasm. The function of HeRs remains unknown. We present the structures of the bacterial HeR-48C12 in two states at the resolution of 1.5 angstrom, which highlight its remarkable difference from all known rhodopsins. The interior of HeR's extracellular part is completely hydrophobic, while the cytoplasmic part comprises a cavity (Schiff base cavity [SBC]) surrounded by charged amino acids and containing a cluster of water molecules, presumably being a primary proton acceptor from the Schiff base. At acidic pH, a planar triangular molecule (acetate) is present in the SBC. Structure-based bioinformatic analysis identified 10 subfamilies of HeRs, suggesting their diverse biological functions. The structures and available data suggest an enzymatic activity of HeR-48C12 subfamily and their possible involvement in fundamental redox biological processes.
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