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Structure paper

TitleCryoRhodopsins: A comprehensive characterization of a group of microbial rhodopsins from cold environments.
Journal, issue, pagesSci Adv, Vol. 11, Issue 27, Page eadv1015, Year 2025
Publish dateJul 4, 2025
AuthorsGerrit H U Lamm / Egor Marin / Alexey Alekseev / Anna V Schellbach / Artem Stetsenko / Jose Manuel Haro-Moreno / Gleb Bourenkov / Valentin Borshchevskiy / Marvin Asido / Michael Agthe / Sylvain Engilberge / Samuel L Rose / Nicolas Caramello / Antoine Royant / Thomas R Schneider / Alex Bateman / Thomas Mager / Tobias Moser / Francisco Rodriguez-Valera / Josef Wachtveitl / Albert Guskov / Kirill Kovalev /
PubMed AbstractMicrobial rhodopsins are omnipresent on Earth; however, the vast majority of them remain uncharacterized. Here, we describe a rhodopsin group found in microorganisms from cold environments, such as ...Microbial rhodopsins are omnipresent on Earth; however, the vast majority of them remain uncharacterized. Here, we describe a rhodopsin group found in microorganisms from cold environments, such as glaciers, denoted as CryoRhodopsins (CryoRs). A distinguishing feature of the group is the presence of a buried arginine residue close to the cytoplasmic face. Combining single-particle cryo-electron microscopy and x-ray crystallography with rhodopsin activation by light, we demonstrate that the arginine stabilizes an ultraviolet (UV)-absorbing intermediate of an extremely slow CryoRhodopsin photocycle. Together with extensive spectroscopic characterization, our investigations on CryoR1 and CryoR2 proteins reveal mechanisms of photoswitching in the identified group. Our data suggest that CryoRs are sensors for UV irradiation and are also capable of inward proton translocation modulated by UV light.
External linksSci Adv / PubMed:40614199 / PubMed Central
MethodsEM (single particle)
Resolution2.3 - 2.94 Å
Structure data

EMDB-18795, PDB-8r0k:
Cryo-EM structure of the microbial rhodopsin CryoR1 at pH 4.3 in detergent
Method: EM (single particle) / Resolution: 2.94 Å

EMDB-18796, PDB-8r0l:
Cryo-EM structure of the microbial rhodopsin CryoR1 at pH 8.0 in nanodisc
Method: EM (single particle) / Resolution: 2.43 Å

EMDB-18797, PDB-8r0m:
Cryo-EM structure of the microbial rhodopsin CryoR1 at pH 8.0 in detergent
Method: EM (single particle) / Resolution: 2.87 Å

EMDB-18798, PDB-8r0n:
Cryo-EM structure of the microbial rhodopsin CryoR1 at pH 10.5 in detergent in the ground state
Method: EM (single particle) / Resolution: 2.7 Å

EMDB-18799, PDB-8r0o:
Cryo-EM structure of the microbial rhodopsin CryoR1 at pH 10.5 in detergent in the M state
Method: EM (single particle) / Resolution: 2.3 Å

EMDB-18800, PDB-8r0p:
Cryo-EM structure of the microbial rhodopsin CryoR2 at pH 8.0 in detergent
Method: EM (single particle) / Resolution: 2.44 Å

Chemicals

ChemComp-LFA:
EICOSANE

ChemComp-RET:
RETINAL

ChemComp-HOH:
WATER

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

Source
  • cryobacterium levicorallinum (bacteria)
  • subtercola endophyticus (bacteria)
KeywordsMEMBRANE PROTEIN / rhodopsin / retinal / cryo-EM / light sensor

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