6GDG

Cryo-EM structure of the adenosine A2A receptor bound to a miniGs heterotrimer

Summary for 6GDG

• Entry DOI: 10.2210/pdb6gdg/pdb
• EMDB information: 4390
• Descriptor: TrxA,Adenosine receptor A2a, Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1, Guanine nucleotide-binding protein G(I)/G(S)/G(O) subunit gamma-2, ... (6 entities in total)
• Functional Keywords: g-protein coupled receptor, adenosine, gpcr, a2a receptor, membrane protein
• Biological source: Escherichia coli; More
• Total number of polymer chains: 5
• Total formula weight: 144182.65

Authors

Garcia-Nafria, J.,Lee, Y. (deposition date: 2018-04-23, release date: 2018-05-16, Last modification date: 2019-12-18)

Primary citation

Garcia-Nafria, J.,Lee, Y.,Bai, X.,Carpenter, B.,Tate, C.G.
Cryo-EM structure of the adenosine A2Areceptor coupled to an engineered heterotrimeric G protein.
Elife, 7:-, 2018

PubMed Abstract: The adenosine A receptor (AR) is a prototypical G protein-coupled receptor (GPCR) that couples to the heterotrimeric G protein G. Here, we determine the structure by electron cryo-microscopy (cryo-EM) of AR at pH 7.5 bound to the small molecule agonist NECA and coupled to an engineered heterotrimeric G protein, which contains mini-G, the βγ subunits and nanobody Nb35. Most regions of the complex have a resolution of ~3.8 Å or better. Comparison with the 3.4 Å resolution crystal structure shows that the receptor and mini-G are virtually identical and that the density of the side chains and ligand are of comparable quality. However, the cryo-EM density map also indicates regions that are flexible in comparison to the crystal structures, which unexpectedly includes regions in the ligand binding pocket. In addition, an interaction between intracellular loop 1 of the receptor and the β subunit of the G protein was observed.

PubMed: 29726815
DOI: 10.7554/eLife.35946

Experimental method

ELECTRON MICROSCOPY (4.11 Å)