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Structure paper

TitleStructural basis for no retinal binding in flotillin-associated rhodopsins.
Journal, issue, pagesStructure, Vol. 33, Issue 9, Page 1462-11469.e3, Year 2025
Publish dateSep 4, 2025
AuthorsKirill Kovalev / Artem Stetsenko / Florian Trunk / Egor Marin / Jose M Haro-Moreno / Gerrit H U Lamm / Alexey Alekseev / Francisco Rodriguez-Valera / Thomas R Schneider / Josef Wachtveitl / Albert Guskov /
PubMed AbstractRhodopsins are light-sensitive membrane proteins capturing solar energy via a retinal cofactor covalently attached to a lysine residue. Several groups of rhodopsins lack the conserved lysine and ...Rhodopsins are light-sensitive membrane proteins capturing solar energy via a retinal cofactor covalently attached to a lysine residue. Several groups of rhodopsins lack the conserved lysine and showed no retinal binding. Recently, flotillin-associated rhodopsins (FArhodopsins or FARs) were identified and suggested to lack the retinal-binding pocket despite preserving the lysine residue in many members of the group. Here, we present cryoelectron microscopic (cryo-EM) structures of paralog FArhodopsin and proteorhodopsin from marine bacterium Pseudothioglobus, both forming pentamers similar to those of other microbial rhodopsins. We demonstrate no binding of retinal to the FArhodopsin despite preservation of the lysine residue and overall similarity of the protein fold and internal organization to those of the retinal-binding paralog. Mutational analysis confirmed that two amino acids, H84 and E120, prevent retinal binding within the FArhodopsin. Our work provides insights into the natural retinal loss in microbial rhodopsins and might contribute to the further understanding of FArhodopsins.
External linksStructure / PubMed:40651474
MethodsEM (single particle)
Resolution2.48 - 2.81 Å
Structure data

53519

9r21

EMDB-53519, PDB-9r21:
Cryo-EM structure of the flotillin-associated rhodopsin PsFAR in detergent micelle
Method: EM (single particle) / Resolution: 2.56 Å

53520

9r22

EMDB-53520, PDB-9r22:
Cryo-EM structure of the light-driven proton pump PsPR in detergent micelle
Method: EM (single particle) / Resolution: 2.48 Å

53521

9r23

EMDB-53521, PDB-9r23:
Cryo-EM structure of the double mutant H84V/E120G of the flotillin-associated rhodopsin PsFAR in detergent micelle
Method: EM (single particle) / Resolution: 2.81 Å

Chemicals

ChemComp-LFA:
EICOSANE

ChemComp-HOH:
WATER

ChemComp-RET:
RETINAL

ChemComp-LMT:
DODECYL-BETA-D-MALTOSIDE / detergent*YM

Source
  • candidatus pseudothioglobus (bacteria)
  • candidatus pseudothioglobus sp. (bacteria)
KeywordsMEMBRANE PROTEIN / flotillin / rhodopsin / retinal / proton transport / bioenergetics / proteorhodopsin / microbial rhodopsin

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