Structural insights into the mechanism of rhodopsin phosphodiesterase

Structural insights into the mechanism of rhodopsin phosphodiesterase

Rhodopsin phosphodiesterase (Rh-PDE) hydrolyzes both cAMP and cGMP in a light-dependent manner. Structural and functional analyses of the Rh-PDE from Salpingoeca rosetta reveal unusual rhodopsin topology comprising 8 transmembrane helices (TMs) and suggest that TM0 plays a crucial role in the enzyma...

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Autores principales: Tatsuya Ikuta, Wataru Shihoya, Masahiro Sugiura, Kazuho Yoshida, Masahito Watari, Takaya Tokano, Keitaro Yamashita, Kota Katayama, Satoshi P. Tsunoda, Takayuki Uchihashi, Hideki Kandori, Osamu Nureki
Formato: article
Lenguaje:EN
Publicado: Nature Portfolio 2020
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Q
Acceso en línea:https://doaj.org/article/951cafa1c8b649b8abf09d8e22b57cbc
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spelling oai:doaj.org-article:951cafa1c8b649b8abf09d8e22b57cbc2021-12-02T15:37:15ZStructural insights into the mechanism of rhodopsin phosphodiesterase10.1038/s41467-020-19376-72041-1723https://doaj.org/article/951cafa1c8b649b8abf09d8e22b57cbc2020-11-01T00:00:00Zhttps://doi.org/10.1038/s41467-020-19376-7https://doaj.org/toc/2041-1723Rhodopsin phosphodiesterase (Rh-PDE) hydrolyzes both cAMP and cGMP in a light-dependent manner. Structural and functional analyses of the Rh-PDE from Salpingoeca rosetta reveal unusual rhodopsin topology comprising 8 transmembrane helices (TMs) and suggest that TM0 plays a crucial role in the enzymatic photoactivity.Tatsuya IkutaWataru ShihoyaMasahiro SugiuraKazuho YoshidaMasahito WatariTakaya TokanoKeitaro YamashitaKota KatayamaSatoshi P. TsunodaTakayuki UchihashiHideki KandoriOsamu NurekiNature PortfolioarticleScienceQENNature Communications, Vol 11, Iss 1, Pp 1-12 (2020)
institution DOAJ
collection DOAJ
language EN
topic Science
Q
spellingShingle Science
Q
Tatsuya Ikuta
Wataru Shihoya
Masahiro Sugiura
Kazuho Yoshida
Masahito Watari
Takaya Tokano
Keitaro Yamashita
Kota Katayama
Satoshi P. Tsunoda
Takayuki Uchihashi
Hideki Kandori
Osamu Nureki
Structural insights into the mechanism of rhodopsin phosphodiesterase
description Rhodopsin phosphodiesterase (Rh-PDE) hydrolyzes both cAMP and cGMP in a light-dependent manner. Structural and functional analyses of the Rh-PDE from Salpingoeca rosetta reveal unusual rhodopsin topology comprising 8 transmembrane helices (TMs) and suggest that TM0 plays a crucial role in the enzymatic photoactivity.
format article
author Tatsuya Ikuta
Wataru Shihoya
Masahiro Sugiura
Kazuho Yoshida
Masahito Watari
Takaya Tokano
Keitaro Yamashita
Kota Katayama
Satoshi P. Tsunoda
Takayuki Uchihashi
Hideki Kandori
Osamu Nureki
author_facet Tatsuya Ikuta
Wataru Shihoya
Masahiro Sugiura
Kazuho Yoshida
Masahito Watari
Takaya Tokano
Keitaro Yamashita
Kota Katayama
Satoshi P. Tsunoda
Takayuki Uchihashi
Hideki Kandori
Osamu Nureki
author_sort Tatsuya Ikuta
title Structural insights into the mechanism of rhodopsin phosphodiesterase
title_short Structural insights into the mechanism of rhodopsin phosphodiesterase
title_full Structural insights into the mechanism of rhodopsin phosphodiesterase
title_fullStr Structural insights into the mechanism of rhodopsin phosphodiesterase
title_full_unstemmed Structural insights into the mechanism of rhodopsin phosphodiesterase
title_sort structural insights into the mechanism of rhodopsin phosphodiesterase
publisher Nature Portfolio
publishDate 2020
url https://doaj.org/article/951cafa1c8b649b8abf09d8e22b57cbc
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