TY  - JOUR
AU  - Kovalev, Kirill
AU  - Volkov, D.
AU  - Astashkin, R.
AU  - Alekseev, Alexey
AU  - Gushchin, I.
AU  - Haro-Moreno, J. M.
AU  - Chizhov, I.
AU  - Siletsky, S.
AU  - Mamedov, M.
AU  - Rogachev, A.
AU  - Balandin, T.
AU  - Borshchevskiy, Valentin
AU  - Popov, A.
AU  - Bourenkov, G.
AU  - Bamberg, E.
AU  - Rodriguez-Valera, F.
AU  - Büldt, G.
AU  - Gordeliy, V.
TI  - High-resolution structural insights into the heliorhodopsin family
JO  - Proceedings of the National Academy of Sciences of the United States of America
VL  - 117
IS  - 8
SN  - 1091-6490
CY  - Washington, DC
PB  - National Acad. of Sciences
M1  - FZJ-2020-01830
SP  - 4131 - 4141
PY  - 2020
AB  - 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 Å, 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.
LB  - PUB:(DE-HGF)16
C6  - pmid:32034096
UR  - <Go to ISI:>//WOS:000516771500038
DO  - DOI:10.1073/pnas.1915888117
UR  - https://juser.fz-juelich.de/record/875138
ER  -