9R21

Cryo-EM structure of the flotillin-associated rhodopsin PsFAR in detergent micelle

Summary for 9R21

• Entry DOI: 10.2210/pdb9r21/pdb
• EMDB information: 53519
• Descriptor: flotillin-associated rhodopsin, EICOSANE (3 entities in total)
• Functional Keywords: flotillin, rhodopsin, retinal, membrane protein
• Biological source: Candidatus Pseudothioglobus
• Total number of polymer chains: 5
• Total formula weight: 160477.53

Authors

Kovalev, K.,Stetsenko, A.,Marin, E.,Guskov, A. (deposition date: 2025-04-29, release date: 2025-07-23)

Primary citation

Kovalev, K.,Stetsenko, A.,Trunk, F.,Marin, E.,Haro-Moreno, J.M.,Lamm, G.H.U.,Alekseev, A.,Rodriguez-Valera, F.,Schneider, T.R.,Wachtveitl, J.,Guskov, A.
Structural basis for no retinal binding in flotillin-associated rhodopsins.
Structure, 2025

PubMed Abstract: 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.

PubMed: 40651474
DOI: 10.1016/j.str.2025.06.006

Experimental method

ELECTRON MICROSCOPY (2.56 Å)