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TitleAllosteric activation of the nitric oxide receptor soluble guanylate cyclase mapped by cryo-electron microscopy.
Journal, issue, pagesElife, Vol. 8, Year 2019
Publish dateSep 30, 2019
AuthorsBenjamin G Horst / Adam L Yokom / Daniel J Rosenberg / Kyle L Morris / Michal Hammel / James H Hurley / Michael A Marletta /
PubMed AbstractSoluble 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 linksElife / PubMed:31566566 / PubMed Central
MethodsEM (single particle)
Resolution5.1 - 5.8 Å
Structure data

20282

6pas

EMDB-20282, PDB-6pas:
Inactive State of Manduca sexta soluble guanylate cyclase
Method: EM (single particle) / Resolution: 5.1 Å

20283

6pat

EMDB-20283, PDB-6pat:
Active State of Manduca sexta soluble Guanylate Cyclase
Method: EM (single particle) / Resolution: 5.8 Å

Chemicals

ChemComp-HEM:
PROTOPORPHYRIN IX CONTAINING FE

Source
  • manduca sexta (tobacco hornworm)
KeywordsSIGNALING PROTEIN / Nitric oxide / cyclase / H-NOX / stimulator

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