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TitleStructure of the class D GPCR Ste2 dimer coupled to two G proteins.
Journal, issue, pagesNature, Vol. 589, Issue 7840, Page 148-153, Year 2021
Publish dateDec 2, 2020
AuthorsVaithish Velazhahan / Ning Ma / Gáspár Pándy-Szekeres / Albert J Kooistra / Yang Lee / David E Gloriam / Nagarajan Vaidehi / Christopher G Tate /
PubMed AbstractG-protein-coupled receptors (GPCRs) are divided phylogenetically into six classes, denoted A to F. More than 370 structures of vertebrate GPCRs (belonging to classes A, B, C and F) have been ...G-protein-coupled receptors (GPCRs) are divided phylogenetically into six classes, denoted A to F. More than 370 structures of vertebrate GPCRs (belonging to classes A, B, C and F) have been determined, leading to a substantial understanding of their function. By contrast, there are no structures of class D GPCRs, which are found exclusively in fungi where they regulate survival and reproduction. Here we determine the structure of a class D GPCR, the Saccharomyces cerevisiae pheromone receptor Ste2, in an active state coupled to the heterotrimeric G protein Gpa1-Ste4-Ste18. Ste2 was purified as a homodimer coupled to two G proteins. The dimer interface of Ste2 is formed by the N terminus, the transmembrane helices H1, H2 and H7, and the first extracellular loop ECL1. We establish a class D1 generic residue numbering system (CD1) to enable comparisons with orthologues and with other GPCR classes. The structure of Ste2 bears similarities in overall topology to class A GPCRs, but the transmembrane helix H4 is shifted by more than 20 Å and the G-protein-binding site is a shallow groove rather than a cleft. The structure provides a template for the design of novel drugs to target fungal GPCRs, which could be used to treat numerous intractable fungal diseases.
External linksNature / PubMed:33268889 / PubMed Central
MethodsEM (single particle)
Resolution2.7 - 3.53 Å
Structure data

11720

7ad3

EMDB-11720, PDB-7ad3:
Class D GPCR Ste2 dimer coupled to two G proteins
Method: EM (single particle) / Resolution: 3.3 Å

13880

7qa8

EMDB-13880, PDB-7qa8:
Structure of the GPCR dimer Ste2 bound to an antagonist
Method: EM (single particle) / Resolution: 2.7 Å

13882

7qb9

EMDB-13882, PDB-7qb9:
Structure of the ligand-free GPCR dimer Ste2
Method: EM (single particle) / Resolution: 3.1 Å

13886

7qbc

EMDB-13886, PDB-7qbc:
Structure of the GPCR dimer Ste2 in the inactive-like state bound to agonist
Method: EM (single particle) / Resolution: 3.53 Å

13887

7qbi

EMDB-13887, PDB-7qbi:
Structure of the GPCR dimer Ste2 in the active-like state bound to agonist
Method: EM (single particle) / Resolution: 3.46 Å

Chemicals

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

ChemComp-Y01:
CHOLESTEROL HEMISUCCINATE

ChemComp-HOH:
WATER

Source
  • saccharomyces cerevisiae (brewer's yeast)
  • saccharomyces cerevisiae (strain atcc 204508 / s288c) (yeast)
KeywordsMEMBRANE PROTEIN / Fungal GPCR / Dimer / Complex / Class D / Active State / GPCR / antagonist-bound / fungal / ligand-free / agonist-bound

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