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-Structure paper
タイトル | The structure of a membrane adenylyl cyclase bound to an activated stimulatory G protein. |
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ジャーナル・号・ページ | Science, Vol. 364, Issue 6438, Page 389-394, Year 2019 |
掲載日 | 2019年4月26日 |
著者 | Chao Qi / Simona Sorrentino / Ohad Medalia / Volodymyr M Korkhov / |
PubMed 要旨 | Membrane-integral adenylyl cyclases (ACs) are key enzymes in mammalian heterotrimeric GTP-binding protein (G protein)-dependent signal transduction, which is important in many cellular processes. ...Membrane-integral adenylyl cyclases (ACs) are key enzymes in mammalian heterotrimeric GTP-binding protein (G protein)-dependent signal transduction, which is important in many cellular processes. Signals received by the G protein-coupled receptors are conveyed to ACs through G proteins to modulate the levels of cellular cyclic adenosine monophosphate (cAMP). Here, we describe the cryo-electron microscopy structure of the bovine membrane AC9 bound to an activated G protein αs subunit at 3.4-angstrom resolution. The structure reveals the organization of the membrane domain and helical domain that spans between the membrane and catalytic domains of AC9. The carboxyl-terminal extension of the catalytic domain occludes both the catalytic and the allosteric sites of AC9, inducing a conformation distinct from the substrate- and activator-bound state, suggesting a regulatory role in cAMP production. |
リンク | Science / PubMed:31023924 |
手法 | EM (単粒子) |
解像度 | 3.1 - 4.2 Å |
構造データ | EMDB-4719, PDB-6r3q: EMDB-4721: Structure of a truncated adenylyl cyclase bound to MANT-GTP, forskolin and an activatedstimulatory Galphas protein EMDB-4722: Structure of a soluble domain of adenylyl cyclase bound to an activatedstimulatory G protein EMDB-4723: EMDB-4724: EMDB-4725: EMDB-4726: |
化合物 | ChemComp-GSP: ChemComp-MG: ChemComp-ONM: ChemComp-FOK: ChemComp-MN: |
由来 |
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キーワード | MEMBRANE PROTEIN / adenylyl cyclase / G protein / occluded state / MANT-GTP / forskolin |