8HTG

Crystal structure of Golf in complex with GTP-gamma S and Mg

8HTG の概要

• エントリーDOI: 10.2210/pdb8htg/pdb
• 分子名称: Guanine nucleotide-binding protein G(olf) subunit alpha, 1,2-ETHANEDIOL, MAGNESIUM ION, ... (6 entities in total)
• 機能のキーワード: g protein, signaling protein
• 由来する生物種: Mus musculus (house mouse)
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 186932.35

構造登録者

Kang, H.,Choi, H.-J. (登録日: 2022-12-21, 公開日: 2023-12-20)

主引用文献

Choi, C.,Bae, J.,Kim, S.,Lee, S.,Kang, H.,Kim, J.,Bang, I.,Kim, K.,Huh, W.K.,Seok, C.,Park, H.,Im, W.,Choi, H.J.
Understanding the molecular mechanisms of odorant binding and activation of the human OR52 family.
Nat Commun, 14:8105-8105, 2023

PubMed Abstract: Structural and mechanistic studies on human odorant receptors (ORs), key in olfactory signaling, are challenging because of their low surface expression in heterologous cells. The recent structure of OR51E2 bound to propionate provided molecular insight into odorant recognition, but the lack of an inactive OR structure limited understanding of the activation mechanism of ORs upon odorant binding. Here, we determined the cryo-electron microscopy structures of consensus OR52 (OR52), a representative of the OR52 family, in the ligand-free (apo) and octanoate-bound states. The apo structure of OR52 reveals a large opening between transmembrane helices (TMs) 5 and 6. A comparison between the apo and active structures of OR52 demonstrates the inward and outward movements of the extracellular and intracellular segments of TM6, respectively. These results, combined with molecular dynamics simulations and signaling assays, shed light on the molecular mechanisms of odorant binding and activation of the OR52 family.

PubMed: 38062020
DOI: 10.1038/s41467-023-43983-9

実験手法

X-RAY DIFFRACTION (2.91 Å)