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...

Full description

Saved in:
Bibliographic Details
Main Authors: 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
Format: article
Language:EN
Published: Nature Portfolio 2020
Subjects:
Science
Q
Online Access:https://doaj.org/article/951cafa1c8b649b8abf09d8e22b57cbc
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary: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.

Similar Items