3RWM

Crystal Structure of Ypt32 in Complex with GppNHp

3RWM の概要

• エントリーDOI: 10.2210/pdb3rwm/pdb
• 関連するPDBエントリー: 3RWO
• 分子名称: GTP-binding protein YPT32/YPT11, PHOSPHOAMINOPHOSPHONIC ACID-GUANYLATE ESTER, MAGNESIUM ION, ... (4 entities in total)
• 機能のキーワード: ypt32, rab gtpase, vesicle trafficking, effectors, myo2p, gppnhp, protein transport
• 由来する生物種: Saccharomyces cerevisiae (Baker's yeast)
• 細胞内の位置: Golgi apparatus membrane; Lipid-anchor: P51996
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 21671.76

構造登録者

Sultana, A.,Dregger, C.,Jin, Y.,Franklin, E.,Weisman, L.S.,Khan, A.R. (登録日: 2011-05-09, 公開日: 2011-10-26, 最終更新日: 2024-02-28)

主引用文献

Sultana, A.,Jin, Y.,Dregger, C.,Franklin, E.,Weisman, L.S.,Khan, A.R.
The activation cycle of Rab GTPase Ypt32 reveals structural determinants of effector recruitment and GDI binding.
Febs Lett., 585:3520-3527, 2011

PubMed Abstract: Rab GTPases localize to distinct sub-cellular compartments and regulate vesicle trafficking in eukaryotic cells. Yeast Rabs Ypt31/32 and Sec4 have 68% homology and bind to common interactors, yet play distinct roles in the transport of exocytic vesicles. The structures of Ypt31/32 have not previously been reported in the uncomplexed state. We describe the crystal structures of GTP and GDP forms of Ypt32 to understand the molecular basis for Rab function. The structure of Ypt32(GTP) reveals that the switch II conformation is distinct from Sec4(GTP) in spite of a highly conserved amino acid sequence. Also, Ypt32(GDP) reveals a remarkable change in conformation of the switch II helix induced by binding to GDI, which has not been described previously.

PubMed: 22024479
DOI: 10.1016/j.febslet.2011.10.013

実験手法

X-RAY DIFFRACTION (2 Å)