6pas | pdb_00006pas

Inactive State of Manduca sexta soluble guanylate cyclase

spinqualitylabelsall models 6pas, resolution 5.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6pas is a 2 chain structure. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: HEM Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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