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Title | Allosteric activation of the nitric oxide receptor soluble guanylate cyclase mapped by cryo-electron microscopy. |
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Journal, issue, pages | Elife, Vol. 8, Year 2019 |
Publish date | Sep 30, 2019 |
Authors | Benjamin G Horst / Adam L Yokom / Daniel J Rosenberg / Kyle L Morris / Michal Hammel / James H Hurley / Michael A Marletta / |
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 ...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. |
External links | Elife / PubMed:31566566 / PubMed Central |
Methods | EM (single particle) |
Resolution | 5.1 - 5.8 Å |
Structure data | EMDB-20282, PDB-6pas: EMDB-20283, PDB-6pat: |
Chemicals | ChemComp-HEM: |
Source |
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Keywords | SIGNALING PROTEIN / Nitric oxide / cyclase / H-NOX / stimulator |