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Structure paper

TitleStructural basis of adenylyl cyclase 9 activation.
Journal, issue, pagesNat Commun, Vol. 13, Issue 1, Page 1045, Year 2022
Publish dateFeb 24, 2022
AuthorsChao Qi / Pia Lavriha / Ved Mehta / Basavraj Khanppnavar / Inayathulla Mohammed / Yong Li / Michalis Lazaratos / Jonas V Schaefer / Birgit Dreier / Andreas Plückthun / Ana-Nicoleta Bondar / Carmen W Dessauer / Volodymyr M Korkhov /
PubMed AbstractAdenylyl cyclase 9 (AC9) is a membrane-bound enzyme that converts ATP into cAMP. The enzyme is weakly activated by forskolin, fully activated by the G protein Gαs subunit and is autoinhibited by the ...Adenylyl cyclase 9 (AC9) is a membrane-bound enzyme that converts ATP into cAMP. The enzyme is weakly activated by forskolin, fully activated by the G protein Gαs subunit and is autoinhibited by the AC9 C-terminus. Although our recent structural studies of the AC9-Gαs complex provided the framework for understanding AC9 autoinhibition, the conformational changes that AC9 undergoes in response to activator binding remains poorly understood. Here, we present the cryo-EM structures of AC9 in several distinct states: (i) AC9 bound to a nucleotide inhibitor MANT-GTP, (ii) bound to an artificial activator (DARPin C4) and MANT-GTP, (iii) bound to DARPin C4 and a nucleotide analogue ATPαS, (iv) bound to Gαs and MANT-GTP. The artificial activator DARPin C4 partially activates AC9 by binding at a site that overlaps with the Gαs binding site. Together with the previously observed occluded and forskolin-bound conformations, structural comparisons of AC9 in the four conformations described here show that secondary structure rearrangements in the region surrounding the forskolin binding site are essential for AC9 activation.
External linksNat Commun / PubMed:35210418 / PubMed Central
MethodsEM (single particle)
Resolution3.8 - 4.9 Å
Structure data

13330

7pd4

EMDB-13330, PDB-7pd4:
structure of Adenylyl cyclase 9 in complex with MANT-GTP
Method: EM (single particle) / Resolution: 4.9 Å

13331

7pd8

EMDB-13331, PDB-7pd8:
Structure of Adenylyl cyclase 9 in complex with DARPin C4 and MANT-GTP
Method: EM (single particle) / Resolution: 4.2 Å

13334

7pdd

EMDB-13334, PDB-7pdd:
Focus refinement of soluble domain of Adenylyl cyclase 9 in complex with DARPin C4 and MANT-GTP
Method: EM (single particle) / Resolution: 4.2 Å

13335

7pde

EMDB-13335, PDB-7pde:
Structure of Adenylyl cyclase 9 in complex with Gs protein alpha subunit and MANT-GTP
Method: EM (single particle) / Resolution: 4.5 Å

13336

7pdf

EMDB-13336, PDB-7pdf:
focus refinement of soluble domain of adenylyl cyclase 9 in complex with Gs protein alpha subunit and MANT-GTP
Method: EM (single particle) / Resolution: 3.8 Å

13337

7pdg

EMDB-13337, PDB-7pdg:
structure of adenylyl cyclase 9 in complex with DARPin C4 and ATP-aS
Method: EM (single particle) / Resolution: 4.3 Å

13338

7pdh

EMDB-13338, PDB-7pdh:
structure of adenylyl cyclase 9 in complex with DARPin C4 and ATP-aS
Method: EM (single particle) / Resolution: 4.0 Å

Chemicals

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

ChemComp-MG:
Unknown entry

Source
  • bos taurus (cattle)
  • synthetic construct (others)
KeywordsSIGNALING PROTEIN / membrane protein / adenylyl cyclase / signalling transduction.

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