6JT1

Structure of human soluble guanylate cyclase in the heme oxidised state

6JT1 の概要

• エントリーDOI: 10.2210/pdb6jt1/pdb
• EMDBエントリー: 9884
• 分子名称: Guanylate cyclase soluble subunit alpha-1, Guanylate cyclase soluble subunit beta-1, PROTOPORPHYRIN IX CONTAINING FE (3 entities in total)
• 機能のキーワード: soluble guanylate cyclase, signaling protein
• 由来する生物種: Homo sapiens (Human); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 148782.29

構造登録者

Chen, L.,Kang, Y.,Liu, R.,Wu, J.-X. (登録日: 2019-04-08, 公開日: 2019-08-28, 最終更新日: 2024-03-27)

主引用文献

Kang, Y.,Liu, R.,Wu, J.X.,Chen, L.
Structural insights into the mechanism of human soluble guanylate cyclase.
Nature, 574:206-210, 2019

PubMed Abstract: Soluble guanylate cyclase (sGC) is the primary sensor of nitric oxide. It has a central role in nitric oxide signalling and has been implicated in many essential physiological processes and disease conditions. The binding of nitric oxide boosts the enzymatic activity of sGC. However, the mechanism by which nitric oxide activates the enzyme is unclear. Here we report the cryo-electron microscopy structures of the human sGCα1β1 heterodimer in different functional states. These structures revealed that the transducer module bridges the nitric oxide sensor module and the catalytic module. Binding of nitric oxide to the β1 haem-nitric oxide and oxygen binding (H-NOX) domain triggers the structural rearrangement of the sensor module and a conformational switch of the transducer module from bending to straightening. The resulting movement of the N termini of the catalytic domains drives structural changes within the catalytic module, which in turn boost the enzymatic activity of sGC.

PubMed: 31514202
DOI: 10.1038/s41586-019-1584-6

実験手法

ELECTRON MICROSCOPY (3.9 Å)