期刊
SCIENCE
卷 364, 期 6438, 页码 389-+出版社
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.aav0778
关键词
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资金
- iNEXT [PID 3200]
- Swiss National Science Foundation [150665, SNSF 31003A_179418]
- ETH [ETH-29 15-1]
- Novartis Foundation for Medical-Biological Research [14C178]
- Maxi Foundation
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 as 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.
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