6PAS

Inactive State of Manduca sexta soluble guanylate cyclase

Summary for 6PAS

• Entry DOI: 10.2210/pdb6pas/pdb
• EMDB information: 20282
• Descriptor: Soluble guanylyl cyclase alpha-1 subunit, Soluble guanylyl cyclase beta-1 subunit, PROTOPORPHYRIN IX CONTAINING FE (3 entities in total)
• Functional Keywords: nitric oxide, cyclase, h-nox, signaling protein
• Biological source: Manduca sexta (Tobacco hawkmoth); More
• Total number of polymer chains: 2
• Total formula weight: 147397.21

Authors

Yokom, A.L.,Horst, B.G.,Marletta, M.A.,Hurley, J.H. (deposition date: 2019-06-11, release date: 2019-10-23, Last modification date: 2024-03-20)

Primary citation

Horst, B.G.,Yokom, A.L.,Rosenberg, D.J.,Morris, K.L.,Hammel, M.,Hurley, J.H.,Marletta, M.A.
Allosteric activation of the nitric oxide receptor soluble guanylate cyclase mapped by cryo-electron microscopy.
Elife, 8:-, 2019

PubMed Abstract: Soluble guanylate cyclase (sGC) is the primary receptor for nitric oxide (NO) in mammalian nitric oxide signaling. We determined structures of full-length sGC in both inactive and active states using cryo-electron microscopy. NO and the sGC-specific stimulator YC-1 induce a 71° rotation of the heme-binding β H-NOX and PAS domains. Repositioning of the β H-NOX domain leads to a straightening of the coiled-coil domains, which, in turn, use the motion to move the catalytic domains into an active conformation. YC-1 binds directly between the β H-NOX domain and the two CC domains. The structural elongation of the particle observed in cryo-EM was corroborated in solution using small angle X-ray scattering (SAXS). These structures delineate the endpoints of the allosteric transition responsible for the major cyclic GMP-dependent physiological effects of NO.

PubMed: 31566566
DOI: 10.7554/eLife.50634

Experimental method

ELECTRON MICROSCOPY (5.1 Å)