3GGY

Crystal Structure of S.cerevisiae Ist1 N-terminal domain

3GGY の概要

• エントリーDOI: 10.2210/pdb3ggy/pdb
• 関連するPDBエントリー: 3GGZ
• 分子名称: Increased sodium tolerance protein 1 (2 entities in total)
• 機能のキーワード: escrt-iii like, phosphoprotein, protein transport, endocytosis
• 由来する生物種: Saccharomyces cerevisiae (brewer's yeast,lager beer yeast,yeast)
• 細胞内の位置: Cytoplasm: P53843
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 44760.33

構造登録者

Xiao, J.,Xu, Z. (登録日: 2009-03-02, 公開日: 2009-09-08, 最終更新日: 2024-02-21)

主引用文献

Xiao, J.,Chen, X.W.,Davies, B.A.,Saltiel, A.R.,Katzmann, D.J.,Xu, Z.
Structural basis of Ist1 function and Ist1-Did2 interaction in the multivesicular body pathway and cytokinesis.
MOLECULAR BIOLOGY OF THE CELL, 20:3514-3524, 2009

PubMed Abstract: The ESCRT machinery functions in several important eukaryotic cellular processes. The AAA-ATPase Vps4 catalyzes disassembly of the ESCRT-III complex and may regulate membrane deformation and vesicle scission as well. Ist1 was proposed to be a regulator of Vps4, but its mechanism of action was unclear. The crystal structure of the N-terminal domain of Ist1 (Ist1NTD) reveals an ESCRT-III subunit-like fold, implicating Ist1 as a divergent ESCRT-III family member. Ist1NTD specifically binds to the ESCRT-III subunit Did2, and cocrystallization of Ist1NTD with a Did2 fragment shows that Ist1 interacts with the Did2 C-terminal MIM1 (MIT-interacting motif 1) via a novel MIM-binding structural motif. This arrangement indicates a mechanism for intermolecular ESCRT-III subunit association and may also suggest one form of ESCRT-III subunit autoinhibition via intramolecular interaction.

PubMed: 19477918
DOI: 10.1091/mbc.E09-05-0403

実験手法

X-RAY DIFFRACTION (1.7 Å)