PDBsum entry 6r3q

Membrane protein

PDB id: 6r3q

Contents

Protein chains

841 a.a.

341 a.a.

Ligands

GSP

Metals

_MG

References listed in PDB file

Key reference

• Title: The structure of a membrane adenylyl cyclase bound to an activated stimulatory g protein.
• Authors: C.Qi, S.Sorrentino, O.Medalia, V.M.Korkhov.
• Ref.: Science, 2019, 364, 389-394. [DOI no: 10.1126/science.aav0778]
• PubMed id: 31023924

Abstract

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.