4GJ4

The Crystal Structure of the soluble Guanylate Cyclase PAS alpha domain from Manduca sexta

4GJ4 の概要

• エントリーDOI: 10.2210/pdb4gj4/pdb
• 分子名称: Soluble guanylyl cyclase alpha-1 subunit, SULFATE ION (3 entities in total)
• 機能のキーワード: nitric oxide, cgmp, yc-1, pas domain, pas fold, allosteric regulation, lyase
• 由来する生物種: Manduca sexta (Carolina sphinx,hornblower,tobacco hawkmoth,tomato hornworm)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 56341.24

構造登録者

Purohit, R.,Montfort, W.R.,Weichsel, A. (登録日: 2012-08-09, 公開日: 2013-08-14, 最終更新日: 2023-09-13)

主引用文献

Purohit, R.,Weichsel, A.,Montfort, W.R.
Crystal structure of the Alpha subunit PAS domain from soluble guanylyl cyclase.
Protein Sci., 22:1439-1444, 2013

PubMed Abstract: Soluble guanylate cyclase (sGC) is a heterodimeric heme protein of ≈ 150 kDa and the primary nitric oxide receptor. Binding of NO stimulates cyclase activity, leading to regulation of cardiovascular physiology and providing attractive opportunities for drug discovery. How sGC is stimulated and where candidate drugs bind remains unknown. The α and β sGC chains are each composed of Heme-Nitric Oxide Oxygen (H-NOX), Per-ARNT-Sim (PAS), coiled-coil and cyclase domains. Here, we present the crystal structure of the α1 PAS domain to 1.8 Å resolution. The structure reveals the binding surfaces of importance to heterodimer function, particularly with respect to regulating NO binding to heme in the β1 H-NOX domain. It also reveals a small internal cavity that may serve to bind ligands or participate in signal transduction.

PubMed: 23934793
DOI: 10.1002/pro.2331

実験手法

X-RAY DIFFRACTION (1.8 Å)