3LXU

Crystal Structure of Tripeptidyl Peptidase 2 (TPP II)

3LXU の概要

• エントリーDOI: 10.2210/pdb3lxu/pdb
• 分子名称: Tripeptidyl-peptidase 2 (1 entity in total)
• 機能のキーワード: spindle complex, aminopeptidase, hydrolase, phosphoprotein, serine protease
• 由来する生物種: Drosophila melanogaster (Fruit fly)
• 細胞内の位置: Cytoplasm (Probable): Q9V6K1
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 150406.61

構造登録者

Chuang, C.K. (登録日: 2010-02-25, 公開日: 2010-08-11, 最終更新日: 2024-10-16)

主引用文献

Chuang, C.K.,Rockel, B.,Seyit, G.,Walian, P.J.,Schonegge, A.M.,Peters, J.,Zwart, P.H.,Baumeister, W.,Jap, B.K.
Hybrid molecular structure of the giant protease tripeptidyl peptidase II.
Nat.Struct.Mol.Biol., 17:990-996, 2010

PubMed Abstract: Tripeptidyl peptidase II (TPP II) is the largest known eukaryotic protease (6 MDa). It is believed to act downstream of the 26S proteasome, cleaving tripeptides from the N termini of longer peptides, and it is implicated in numerous cellular processes. Here we report the structure of Drosophila TPP II determined by a hybrid approach. We solved the structure of the dimer by X-ray crystallography and docked it into the three-dimensional map of the holocomplex, which we obtained by single-particle cryo-electron microscopy. The resulting structure reveals the compartmentalization of the active sites inside a system of chambers and suggests the existence of a molecular ruler determining the size of the cleavage products. Furthermore, the structure suggests a model for activation of TPP II involving the relocation of a flexible loop and a repositioning of the active-site serine, coupling it to holocomplex assembly and active-site sequestration.

PubMed: 20676100
DOI: 10.1038/nsmb.1870

実験手法

X-RAY DIFFRACTION (3.14 Å)