TY - JOUR
T1 - Unique structure and function of viral rhodopsins
AU - Bratanov, Dmitry
AU - Kovalev, Kirill
AU - Machtens, Jan-Philipp
AU - Astashkin, Roman
AU - Chizhov, Igor
AU - Soloviov, Dmytro
AU - Volkov, Dmytro
AU - Polovinkin, Vitaly
AU - Zabelskii, Dmitrii
AU - Mager, Thomas
AU - Gushchin, Ivan
AU - Rokitskaya, Tatyana
AU - Antonenko, Yuri
AU - Alekseev, Alexey
AU - Shevchenko, Vitaly
AU - Yutin, Natalya
AU - Rosselli, Riccardo
AU - Baeken, Christian
AU - Borshchevskiy, Valentin
AU - Bourenkov, Gleb
AU - Popov, Alexander
AU - Balandin, Taras
AU - Büldt, Georg
AU - Manstein, Dietmar J.
AU - Rodriguez-Valera, Francisco
AU - Fahlke, Christoph
AU - Bamberg, Ernst
AU - Koonin, Eugene
AU - Gordeliy, Valentin
PY - 2019/12/1
Y1 - 2019/12/1
N2 - Recently, two groups of rhodopsin genes were identified in large double-stranded DNA viruses. The structure and function of viral rhodopsins are unknown. We present functional characterization and high-resolution structure of an Organic Lake Phycodnavirus rhodopsin II (OLPVRII) of group 2. It forms a pentamer, with a symmetrical, bottle-like central channel with the narrow vestibule in the cytoplasmic part covered by a ring of 5 arginines, whereas 5 phenylalanines form a hydrophobic barrier in its exit. The proton donor E42 is placed in the helix B. The structure is unique among the known rhodopsins. Structural and functional data and molecular dynamics suggest that OLPVRII might be a light-gated pentameric ion channel analogous to pentameric ligand-gated ion channels, however, future patch clamp experiments should prove this directly. The data shed light on a fundamentally distinct branch of rhodopsins and may contribute to the understanding of virus-host interactions in ecologically important marine protists.
AB - Recently, two groups of rhodopsin genes were identified in large double-stranded DNA viruses. The structure and function of viral rhodopsins are unknown. We present functional characterization and high-resolution structure of an Organic Lake Phycodnavirus rhodopsin II (OLPVRII) of group 2. It forms a pentamer, with a symmetrical, bottle-like central channel with the narrow vestibule in the cytoplasmic part covered by a ring of 5 arginines, whereas 5 phenylalanines form a hydrophobic barrier in its exit. The proton donor E42 is placed in the helix B. The structure is unique among the known rhodopsins. Structural and functional data and molecular dynamics suggest that OLPVRII might be a light-gated pentameric ion channel analogous to pentameric ligand-gated ion channels, however, future patch clamp experiments should prove this directly. The data shed light on a fundamentally distinct branch of rhodopsins and may contribute to the understanding of virus-host interactions in ecologically important marine protists.
UR - https://www.scopus.com/pages/publications/85074299472
U2 - 10.1038/s41467-019-12718-0
DO - 10.1038/s41467-019-12718-0
M3 - Article
SN - 2041-1723
VL - 10
JO - Nature Communications
JF - Nature Communications
IS - 1
M1 - 4939
ER -