3CPH

Crystal structure of Sec4 in complex with Rab-GDI

3CPH の概要

• エントリーDOI: 10.2210/pdb3cph/pdb
• 関連するPDBエントリー: 3CPI 3CPJ
• 分子名称: Rab GDP-dissociation inhibitor, Ras-related protein SEC4, MAGNESIUM ION, ... (5 entities in total)
• 機能のキーワード: rab gtpase, prenylation, vesicular transport, cytoplasm, cytoplasmic vesicle, exocytosis, gtp-binding, lipoprotein, membrane, nucleotide-binding, palmitate, phosphoprotein, protein transport, gtpase activation
• 由来する生物種: Saccharomyces cerevisiae (baker's yeast); 詳細
• 細胞内の位置: Cytoplasmic vesicle, secretory vesicle membrane; Lipid-anchor; Cytoplasmic side: P39958; Cytoplasm: P07560
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 126336.36

構造登録者

Kravchenko, S.,Ignatev, A.,Goody, R.S.,Rak, A.,Pylypenko, O. (登録日: 2008-03-31, 公開日: 2008-05-06, 最終更新日: 2023-11-01)

主引用文献

Ignatev, A.,Kravchenko, S.,Rak, A.,Goody, R.S.,Pylypenko, O.
A structural model of the GDP dissociation inhibitor rab membrane extraction mechanism.
J.Biol.Chem., 283:18377-18384, 2008

PubMed Abstract: Rab GDP dissociation inhibitors (GDI)-facilitated extraction of prenylated Rab proteins from membranes plays an important role in vesicular membrane trafficking. The investigated thermodynamic properties of yeast Rab.GDI and Rab.MRS6 complexes demonstrated differences in the Rab binding properties of the closely related Rab GDI and MRS6 proteins, consistent with their functional diversity. The importance of the Rab C terminus and its prenylation for GDI/MRS6 binding was demonstrated using both biochemical and structural data. The presented structures of the apo-form yeast Rab GDI and its two complexes with unprenylated Rab proteins, together with the earlier published structures of the prenylated Ypt1.GDI, provide evidence of allosteric regulation of the GDI lipid binding site opening, which plays a key role in the proposed mechanism of GDI-mediated Rab extraction. We suggest a model for the interaction of GDI with prenylated Rab proteins that incorporates a stepwise increase in affinity as the three different partial interactions are successively formed.

PubMed: 18426803
DOI: 10.1074/jbc.M709718200

実験手法

X-RAY DIFFRACTION (2.9 Å)