3ZS8

S. cerevisiae Get3 complexed with a cytosolic Get1 fragment

3ZS8 の概要

• エントリーDOI: 10.2210/pdb3zs8/pdb
• 関連するPDBエントリー: 2WOJ 3ZS9
• 分子名称: ATPASE GET3, GOLGI TO ER TRAFFIC PROTEIN 1, ZINC ION (3 entities in total)
• 機能のキーワード: hydrolase-transport protein complex, membrane protein, targeting factor, hydrolase/transport protein
• 由来する生物種: SACCHAROMYCES CEREVISIAE (BAKER'S YEAST); 詳細
• 細胞内の位置: Cytoplasm: Q12154; Endoplasmic reticulum membrane; Multi-pass membrane protein: P53192
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 98981.29

構造登録者

Mariappan, M.,Mateja, A.,Dobosz, M.,Bove, E.,Hegde, R.S.,Keenan, R.J. (登録日: 2011-06-24, 公開日: 2011-09-07, 最終更新日: 2023-12-20)

主引用文献

Mariappan, M.,Mateja, A.,Dobosz, M.,Bove, E.,Hegde, R.S.,Keenan, R.J.
The Mechanism of Membrane-Associated Steps in Tail-Anchored Protein Insertion.
Nature, 477:61-, 2011

PubMed Abstract: Tail-anchored (TA) membrane proteins destined for the endoplasmic reticulum are chaperoned by cytosolic targeting factors that deliver them to a membrane receptor for insertion. Although a basic framework for TA protein recognition is now emerging, the decisive targeting and membrane insertion steps are not understood. Here we reconstitute the TA protein insertion cycle with purified components, present crystal structures of key complexes between these components and perform mutational analyses based on the structures. We show that a committed targeting complex, formed by a TA protein bound to the chaperone ATPase Get3, is initially recruited to the membrane through an interaction with Get2. Once the targeting complex has been recruited, Get1 interacts with Get3 to drive TA protein release in an ATPase-dependent reaction. After releasing its TA protein cargo, the now-vacant Get3 recycles back to the cytosol concomitant with ATP binding. This work provides a detailed structural and mechanistic framework for the minimal TA protein insertion cycle.

PubMed: 21866104
DOI: 10.1038/NATURE10362

実験手法

X-RAY DIFFRACTION (3 Å)