4GJ4

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

Summary for 4GJ4

• Entry DOI: 10.2210/pdb4gj4/pdb
• Descriptor: Soluble guanylyl cyclase alpha-1 subunit, SULFATE ION (3 entities in total)
• Functional Keywords: nitric oxide, cgmp, yc-1, pas domain, pas fold, allosteric regulation, lyase
• Biological source: Manduca sexta (Carolina sphinx,hornblower,tobacco hawkmoth,tomato hornworm)
• Total number of polymer chains: 4
• Total formula weight: 56341.24

Authors

Purohit, R.,Montfort, W.R.,Weichsel, A. (deposition date: 2012-08-09, release date: 2013-08-14, Last modification date: 2023-09-13)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.8 Å)