8CXO

Cryo-EM structure of the unliganded mSMO-PGS2 in a lipidic environment

8CXO の概要

• エントリーDOI: 10.2210/pdb8cxo/pdb
• EMDBエントリー: 27062 27063
• 分子名称: Smoothened homolog, GlgA glycogen synthase chimera, CHOLESTEROL (2 entities in total)
• 機能のキーワード: g-protein coupled receptor, smoothened, unliganded state, lipid system, membrane protein
• 由来する生物種: Mus musculus (house mouse); 詳細
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 81254.83

構造登録者

Zhang, K.,Wu, H.,Hoppe, N.,Manglik, A.,Cheng, Y. (登録日: 2022-05-22, 公開日: 2022-08-03, 最終更新日: 2024-10-09)

主引用文献

Zhang, K.,Wu, H.,Hoppe, N.,Manglik, A.,Cheng, Y.
Fusion protein strategies for cryo-EM study of G protein-coupled receptors.
Nat Commun, 13:4366-4366, 2022

PubMed Abstract: Single particle cryogenic-electron microscopy (cryo-EM) is used extensively to determine structures of activated G protein-coupled receptors (GPCRs) in complex with G proteins or arrestins. However, applying it to GPCRs without signaling proteins remains challenging because most receptors lack structural features in their soluble domains to facilitate image alignment. In GPCR crystallography, inserting a fusion protein between transmembrane helices 5 and 6 is a highly successful strategy for crystallization. Although a similar strategy has the potential to broadly facilitate cryo-EM structure determination of GPCRs alone without signaling protein, the critical determinants that make this approach successful are not yet clear. Here, we address this shortcoming by exploring different fusion protein designs, which lead to structures of antagonist bound A adenosine receptor at 3.4 Å resolution and unliganded Smoothened at 3.7 Å resolution. The fusion strategies explored here are likely applicable to cryo-EM interrogation of other GPCRs and small integral membrane proteins.

PubMed: 35902590
DOI: 10.1038/s41467-022-32125-2

実験手法

ELECTRON MICROSCOPY (3.7 Å)