2BCG

Structure of doubly prenylated Ypt1:GDI complex

2BCG の概要

• エントリーDOI: 10.2210/pdb2bcg/pdb
• 関連するPDBエントリー: 1ukv
• 分子名称: Secretory pathway GDP dissociation inhibitor, GTP-binding protein YPT1, GERAN-8-YL GERAN, ... (7 entities in total)
• 機能のキーワード: rabgtpase, geranylgeranylation, vesicular transport, protein transport
• 由来する生物種: Saccharomyces cerevisiae (baker's yeast); 詳細
• 細胞内の位置: Cytoplasm : P39958; Endoplasmic reticulum membrane ; Peripheral membrane protein : P01123
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 75891.36

構造登録者

Pylypenko, O.,Rak, A.,Alexandrov, K. (登録日: 2005-10-19, 公開日: 2006-01-17, 最終更新日: 2023-08-23)

主引用文献

Pylypenko, O.,Rak, A.,Durek, T.,Kushnir, S.,Dursina, B.E.,Thomae, N.H.,Constantinescu, A.T.,Brunsveld, L.,Watzke, A.,Waldmann, H.,Goody, R.S.,Alexandrov, K.
Structure of doubly prenylated Ypt1:GDI complex and the mechanism of GDI-mediated Rab recycling
Embo J., 25:13-23, 2006

PubMed Abstract: In eukaryotic cells Rab/Ypt GTPases represent a family of key membrane traffic controllers that associate with their targeted membranes via C-terminally conjugated geranylgeranyl groups. GDP dissociation inhibitor (GDI) is a general and essential regulator of Rab recycling that extracts prenylated Rab proteins from membranes at the end of their cycle of activity and facilitates their delivery to the donor membranes. Here, we present the structure of a complex between GDI and a doubly prenylated Rab protein. We show that one geranylgeranyl residue is deeply buried in a hydrophobic pocket formed by domain II of GDI, whereas the other lipid is more exposed to solvent and is skewed across several atoms of the first moiety. Based on structural information and biophysical measurements, we propose mechanistic and thermodynamic models for GDI and Rab escort protein-mediated interaction of RabGTPase with intracellular membranes.

PubMed: 16395334
DOI: 10.1038/sj.emboj.7600921

実験手法

X-RAY DIFFRACTION (1.48 Å)