3B2E

Crystal structure of S. cerevisiae Get3 in the open conformation in complex with Get1 cytosolic domain

3B2E の概要

• エントリーDOI: 10.2210/pdb3b2e/pdb
• 関連するPDBエントリー: 3VLC
• 分子名称: ATPase GET3, Golgi to ER traffic protein 1, ADENOSINE-5'-DIPHOSPHATE (3 entities in total)
• 機能のキーワード: protein-protein interaction, receptor complex, hydrolase, transport protein, adp binding, coild-coil, hydrolase-transport protein complex, hydrolase/transport protein
• 由来する生物種: Saccharomyces cerevisiae (yeast); 詳細
• 細胞内の位置: Endoplasmic reticulum membrane; Multi-pass membrane protein: P53192
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 204057.26

構造登録者

Kubota, K.,Yamagata, A.,Fukai, S. (登録日: 2011-07-30, 公開日: 2012-06-27, 最終更新日: 2023-11-01)

主引用文献

Kubota, K.,Yamagata, A.,Sato, Y.,Goto-Ito, S.,Fukai, S.
Get1 stabilizes an open dimer conformation of get3 ATPase by binding two distinct interfaces
J.Mol.Biol., 422:366-375, 2012

PubMed Abstract: Tail-anchored (TA) proteins are integral membrane proteins that possess a single transmembrane domain near their carboxy terminus. TA proteins play critical roles in many important cellular processes such as membrane trafficking, protein translocation, and apoptosis. The GET complex mediates posttranslational insertion of newly synthesized TA proteins to the endoplasmic reticulum membrane. The GET complex is composed of the homodimeric Get3 ATPase and its heterooligomeric receptor, Get1/2. During insertion, the Get3 dimer shuttles between open and closed conformational states, coupled with ATP hydrolysis and the binding/release of TA proteins. We report crystal structures of ADP-bound Get3 in complex with the cytoplasmic domain of Get1 (Get1CD) in open and semi-open conformations at 3.0- and 4.5-Å resolutions, respectively. Our structures and biochemical data suggest that Get1 uses two interfaces to stabilize the open dimer conformation of Get3. We propose that one interface is sufficient for binding of Get1 by Get3, while the second interface stabilizes the open dimer conformation of Get3.

PubMed: 22684149
DOI: 10.1016/j.jmb.2012.05.045

実験手法

X-RAY DIFFRACTION (3 Å)