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-Structure paper
タイトル | Allosteric activation of the nitric oxide receptor soluble guanylate cyclase mapped by cryo-electron microscopy. |
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ジャーナル・号・ページ | Elife, Vol. 8, Year 2019 |
掲載日 | 2019年9月30日 |
著者 | Benjamin G Horst / Adam L Yokom / Daniel J Rosenberg / Kyle L Morris / Michal Hammel / James H Hurley / Michael A Marletta / |
PubMed 要旨 | 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. |
リンク | Elife / PubMed:31566566 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 5.1 - 5.8 Å |
構造データ | EMDB-20282, PDB-6pas: EMDB-20283, PDB-6pat: |
化合物 | ChemComp-HEM: |
由来 |
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キーワード | SIGNALING PROTEIN / Nitric oxide / cyclase / H-NOX / stimulator |