7KMT

Structure of the yeast TRAPPIII-Ypt1(Rab1) complex

7KMT の概要

• エントリーDOI: 10.2210/pdb7kmt/pdb
• EMDBエントリー: 22928
• 分子名称: Trafficking protein particle complex subunit 23, Trafficking protein particle complex subunit 31, Trafficking protein particle complex subunit BET5, ... (9 entities in total)
• 機能のキーワード: gtpase, gef, er, golgi, autophagy, protein transport
• 由来する生物種: Saccharomyces cerevisiae (Baker's yeast); 詳細
• タンパク質・核酸の鎖数: 9
• 化学式量合計: 276514.23

構造登録者

Joiner, A.M.N.,Phillips, B.P.,Miller, E.A.,Fromme, J.C. (登録日: 2020-11-03, 公開日: 2021-06-02, 最終更新日: 2024-10-16)

主引用文献

Joiner, A.M.,Phillips, B.P.,Yugandhar, K.,Sanford, E.J.,Smolka, M.B.,Yu, H.,Miller, E.A.,Fromme, J.C.
Structural basis of TRAPPIII-mediated Rab1 activation.
Embo J., 40:e107607-e107607, 2021

PubMed Abstract: The GTPase Rab1 is a master regulator of the early secretory pathway and is critical for autophagy. Rab1 activation is controlled by its guanine nucleotide exchange factor, the multisubunit TRAPPIII complex. Here, we report the 3.7 Å cryo-EM structure of the Saccharomyces cerevisiae TRAPPIII complex bound to its substrate Rab1/Ypt1. The structure reveals the binding site for the Rab1/Ypt1 hypervariable domain, leading to a model for how the complex interacts with membranes during the activation reaction. We determined that stable membrane binding by the TRAPPIII complex is required for robust activation of Rab1/Ypt1 in vitro and in vivo, and is mediated by a conserved amphipathic α-helix within the regulatory Trs85 subunit. Our results show that the Trs85 subunit serves as a membrane anchor, via its amphipathic helix, for the entire TRAPPIII complex. These findings provide a structural understanding of Rab activation on organelle and vesicle membranes.

PubMed: 34018207
DOI: 10.15252/embj.2020107607

実験手法

ELECTRON MICROSCOPY (3.7 Å)