7UTH

Gea2 open/open conformation (composite structure)

7UTH の概要

• エントリーDOI: 10.2210/pdb7uth/pdb
• 関連するPDBエントリー: 7URO 7URR
• EMDBエントリー: 26749 26750 26751 26752 26753 26754 26755 26765 26766 26769 26770 26771
• 分子名称: GEA2 isoform 1 (1 entity in total)
• 機能のキーワード: gef, protein transport
• 由来する生物種: Saccharomyces cerevisiae (baker's yeast)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 331693.69

構造登録者

Muccini, A.,Fromme, J.C. (登録日: 2022-04-26, 公開日: 2022-08-24, 最終更新日: 2024-06-12)

主引用文献

Muccini, A.J.,Gustafson, M.A.,Fromme, J.C.
Structural basis for activation of Arf1 at the Golgi complex.
Cell Rep, 40:111282-111282, 2022

PubMed Abstract: The Golgi complex is the central sorting station of the eukaryotic secretory pathway. Traffic through the Golgi requires activation of Arf guanosine triphosphatases that orchestrate cargo sorting and vesicle formation by recruiting an array of effector proteins. Arf activation and Golgi membrane association is controlled by large guanine nucleotide exchange factors (GEFs) possessing multiple conserved regulatory domains. Here we present cryoelectron microscopy (cryoEM) structures of full-length Gea2, the yeast paralog of the human Arf-GEF GBF1, that reveal the organization of these regulatory domains and explain how Gea2 binds to the Golgi membrane surface. We find that the GEF domain adopts two different conformations compatible with different stages of the Arf activation reaction. The structure of a Gea2-Arf1 activation intermediate suggests that the movement of the GEF domain primes Arf1 for membrane insertion upon guanosine triphosphate binding. We propose that conformational switching of Gea2 during the nucleotide exchange reaction promotes membrane insertion of Arf1.

PubMed: 36044848
DOI: 10.1016/j.celrep.2022.111282

実験手法

ELECTRON MICROSCOPY (3.9 Å)