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TitleRegulatory sites of CaM-sensitive adenylyl cyclase AC8 revealed by cryo-EM and structural proteomics.
Journal, issue, pagesEMBO Rep, Vol. 25, Issue 3, Page 1513-1540, Year 2024
Publish dateFeb 13, 2024
AuthorsBasavraj Khanppnavar / Dina Schuster / Pia Lavriha / Federico Uliana / Merve Özel / Ved Mehta / Alexander Leitner / Paola Picotti / Volodymyr M Korkhov /
PubMed AbstractMembrane adenylyl cyclase AC8 is regulated by G proteins and calmodulin (CaM), mediating the crosstalk between the cAMP pathway and Ca signalling. Despite the importance of AC8 in physiology, the ...Membrane adenylyl cyclase AC8 is regulated by G proteins and calmodulin (CaM), mediating the crosstalk between the cAMP pathway and Ca signalling. Despite the importance of AC8 in physiology, the structural basis of its regulation by G proteins and CaM is not well defined. Here, we report the 3.5 Å resolution cryo-EM structure of the bovine AC8 bound to the stimulatory Gαs protein in the presence of Ca/CaM. The structure reveals the architecture of the ordered AC8 domains bound to Gαs and the small molecule activator forskolin. The extracellular surface of AC8 features a negatively charged pocket, a potential site for unknown interactors. Despite the well-resolved forskolin density, the captured state of AC8 does not favour tight nucleotide binding. The structural proteomics approaches, limited proteolysis and crosslinking mass spectrometry (LiP-MS and XL-MS), allowed us to identify the contact sites between AC8 and its regulators, CaM, Gαs, and Gβγ, as well as to infer the conformational changes induced by these interactions. Our results provide a framework for understanding the role of flexible regions in the mechanism of AC regulation.
External linksEMBO Rep / PubMed:38351373 / PubMed Central
MethodsEM (single particle)
Resolution3.38 - 4.13 Å
Structure data

EMDB-16249: Structure of Adenylyl cyclase 8 bound to stimulatory G protein, Forskolin, ATPalphaS, and Ca2+/Calmodulin in lipid nanodisc
Method: EM (single particle) / Resolution: 3.97 Å

16252

8buz

EMDB-16252, PDB-8buz:
Structure of Adenylyl cyclase 8 bound to stimulatory G-protein, Ca2+/Calmodulin, Forskolin and MANT-GTP
Method: EM (single particle) / Resolution: 3.5 Å

EMDB-16253: Focused refinement of soluble domain of Adenylyl cyclase 8 bound to stimulatory G-protein, Ca2+/Calmodulin, Forskolin and MANT-GTP
Method: EM (single particle) / Resolution: 3.38 Å

EMDB-16254: Focused refinement of transmembrane domain of Adenylyl cyclase 8 bound to stimulatory G-protein, Ca2+/Calmodulin, Forskolin and MANT-GTP
Method: EM (single particle) / Resolution: 4.13 Å

16255

8bv5

EMDB-16255, PDB-8bv5:
Focus refinement of soluble domain of Adenylyl cyclase 8 bound to stimulatory G protein, Forskolin, ATPalphaS, and Ca2+/Calmodulin in lipid nanodisc conditions
Method: EM (single particle) / Resolution: 3.54 Å

Chemicals

ChemComp-FOK:
FORSKOLIN

ChemComp-GSP:
5'-GUANOSINE-DIPHOSPHATE-MONOTHIOPHOSPHATE

ChemComp-MG:
Unknown entry

Source
  • bos taurus (cattle)
KeywordsMEMBRANE PROTEIN / Adenylyl Cyclase / cAMP signaling / G proteins / Calmodulin

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