3SJD

Crystal structure of S. cerevisiae Get3 with bound ADP-Mg2+ in complex with Get2 cytosolic domain

3SJD の概要

• エントリーDOI: 10.2210/pdb3sjd/pdb
• 関連するPDBエントリー: 3SJA 3SJB 3SJC
• 分子名称: ATPase GET3, Golgi to ER traffic protein 2, ADENOSINE-5'-DIPHOSPHATE, ... (5 entities in total)
• 機能のキーワード: atpase, receptor complex, ta-protein biogenesis, get pathway, hydrolase-transport protein complex, 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: P40056
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 133856.14

構造登録者

Reitz, S.,Wild, K.,Sinning, I. (登録日: 2011-06-21, 公開日: 2011-07-13, 最終更新日: 2024-02-28)

主引用文献

Stefer, S.,Reitz, S.,Wang, F.,Wild, K.,Pang, Y.Y.,Schwarz, D.,Bomke, J.,Hein, C.,Lohr, F.,Bernhard, F.,Denic, V.,Dotsch, V.,Sinning, I.
Structural basis for tail-anchored membrane protein biogenesis by the Get3-receptor complex.
Science, 333:758-762, 2011

PubMed Abstract: Tail-anchored (TA) proteins are involved in cellular processes including trafficking, degradation, and apoptosis. They contain a C-terminal membrane anchor and are posttranslationally delivered to the endoplasmic reticulum (ER) membrane by the Get3 adenosine triphosphatase interacting with the hetero-oligomeric Get1/2 receptor. We have determined crystal structures of Get3 in complex with the cytosolic domains of Get1 and Get2 in different functional states at 3.0, 3.2, and 4.6 angstrom resolution. The structural data, together with biochemical experiments, show that Get1 and Get2 use adjacent, partially overlapping binding sites and that both can bind simultaneously to Get3. Docking to the Get1/2 complex allows for conformational changes in Get3 that are required for TA protein insertion. These data suggest a molecular mechanism for nucleotide-regulated delivery of TA proteins.

PubMed: 21719644
DOI: 10.1126/science.1207125

実験手法

X-RAY DIFFRACTION (4.6 Å)