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Publication Abstract from PubMed

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 alphas 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.

The structure of a membrane adenylyl cyclase bound to an activated stimulatory G protein.,Qi C, Sorrentino S, Medalia O, Korkhov VM Science. 2019 Apr 26;364(6438):389-394. doi: 10.1126/science.aav0778. PMID:31023924^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.