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Unique structure and function of viral rhodopsins.
Nature Communications ( IF 14.7 ) Pub Date : 2019-10-30 , DOI: 10.1038/s41467-019-12718-0
Dmitry Bratanov 1, 2, 3 , Kirill Kovalev 1, 2, 3, 4, 5, 6 , Jan-Philipp Machtens 6, 7 , Roman Astashkin 3, 4 , Igor Chizhov 8 , Dmytro Soloviov 4, 9, 10, 11 , Dmytro Volkov 1, 2, 4 , Vitaly Polovinkin 1, 3 , Dmitrii Zabelskii 1, 2, 4 , Thomas Mager 12 , Ivan Gushchin 4 , Tatyana Rokitskaya 13 , Yuri Antonenko 13 , Alexey Alekseev 1, 2, 4, 5 , Vitaly Shevchenko 1, 2, 4, 5 , Natalya Yutin 14 , Riccardo Rosselli 15 , Christian Baeken 1, 2 , Valentin Borshchevskiy 1, 2, 4 , Gleb Bourenkov 16 , Alexander Popov 17 , Taras Balandin 1, 2 , Georg Büldt 4 , Dietmar J Manstein 8 , Francisco Rodriguez-Valera 15 , Christoph Fahlke 4, 6 , Ernst Bamberg 4, 12 , Eugene Koonin 14 , Valentin Gordeliy 1, 2, 3, 4
Affiliation  

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.

中文翻译:

病毒视紫红质的独特结构和功能。

最近,在大型双链DNA病毒中鉴定出两组视紫红质基因。病毒视紫红质的结构和功能尚不清楚。我们目前的功能表征和高分辨率的结构的有机湖泊藻类视紫红质II(OLPVRII)组2。它形成一个五聚体,具有对称的瓶状中央通道,细胞质部分中的狭窄前庭被一个环覆盖。 5个精氨酸,而5个苯丙氨酸在其出口形成疏水性屏障。质子供体E42位于螺旋B中。结构在已知的视紫红质中是独特的。结构和功能数据以及分子动力学表明,OLPVRII可能是类似于五聚体配体门控离子通道的轻门五聚离子通道,但是,未来的膜片钳实验应直接证明这一点。
更新日期:2019-10-30
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