9CXG

Structure of PDE6C in complex with inhibitory cone p gamma in the presence of cGMP

9CXG の概要

• エントリーDOI: 10.2210/pdb9cxg/pdb
• EMDBエントリー: 45990
• 分子名称: Cone cGMP-specific 3',5'-cyclic phosphodiesterase subunit alpha', cone P gamma, CYCLIC GUANOSINE MONOPHOSPHATE, ... (6 entities in total)
• 機能のキーワード: pde6c, hydrolase
• 由来する生物種: Homo sapiens (human); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 223437.11

構造登録者

Srivastava, D.,Singh, S.,Artemyev, N. (登録日: 2024-07-31, 公開日: 2024-12-18, 最終更新日: 2025-05-21)

主引用文献

Singh, S.,Srivastava, D.,Boyd, K.,Artemyev, N.O.
Structural and functional dynamics of human cone cGMP-phosphodiesterase important for photopic vision.
Proc.Natl.Acad.Sci.USA, 122:e2419732121-e2419732121, 2025

PubMed Abstract: Cone cGMP-phosphodiesterase (PDE6) is the key effector enzyme for daylight vision, and its properties are critical for shaping distinct physiology of cone photoreceptors. We determined the structures of human cone PDE6C in various liganded states by single-particle cryo-EM that reveal essential functional dynamics and adaptations of the enzyme. Our analysis exposed the dynamic nature of PDE6C association with its regulatory γ-subunit (Pγ) which allows openings of the catalytic pocket in the absence of phototransduction signaling, thereby controlling photoreceptor noise and sensitivity. We demonstrate evolutionarily recent adaptations of PDE6C stemming from residue substitutions in the Pγ subunit and the noncatalytic cGMP binding site and influencing the Pγ dynamics in holoPDE6C. Thus, our structural analysis sheds light on the previously unrecognized molecular evolution of the effector enzyme in cones that advances adaptation for photopic vision.

PubMed: 39739818
DOI: 10.1073/pnas.2419732121

実験手法

ELECTRON MICROSCOPY (3 Å)