Structural highlights
6r4o is a 2 chain structure with sequence from Bovin. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
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| Ligands: | , , , , |
| Gene: | ADCY9, BOS_22626 (BOVIN), GNAS, GNAS1 (BOVIN) |
| Resources: | FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT |
Function
[GNAS2_BOVIN] Guanine nucleotide-binding proteins (G proteins) are involved as modulators or transducers in various transmembrane signaling systems. The G(s) protein is involved in hormonal regulation of adenylate cyclase: it activates the cyclase in response to beta-adrenergic stimuli.
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.
References
- ↑ Qi C, Sorrentino S, Medalia O, Korkhov VM. The structure of a membrane adenylyl cyclase bound to an activated stimulatory G protein. Science. 2019 Apr 26;364(6438):389-394. doi: 10.1126/science.aav0778. PMID:31023924 doi:http://dx.doi.org/10.1126/science.aav0778
