Structural highlights
Publication Abstract from PubMed
Soluble guanylate cyclase (sGC) is the primary receptor for nitric oxide (NO) in mammalian nitric oxide signaling. We determined structures of full-length Manduca sexta sGC in both inactive and active states using cryo-electron microscopy. NO and the sGC-specific stimulator YC-1 induce a 71 degrees rotation of the heme-binding beta H-NOX and PAS domains. Repositioning of the beta 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 beta 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.
Allosteric activation of the nitric oxide receptor soluble guanylate cyclase mapped by cryo-electron microscopy.,Horst BG, Yokom AL, Rosenberg DJ, Morris KL, Hammel M, Hurley JH, Marletta MA Elife. 2019 Sep 30;8. pii: 50634. doi: 10.7554/eLife.50634. PMID:31566566[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Horst BG, Yokom AL, Rosenberg DJ, Morris KL, Hammel M, Hurley JH, Marletta MA. Allosteric activation of the nitric oxide receptor soluble guanylate cyclase mapped by cryo-electron microscopy. Elife. 2019 Sep 30;8. pii: 50634. doi: 10.7554/eLife.50634. PMID:31566566 doi:http://dx.doi.org/10.7554/eLife.50634
