6JZC

Structural basis of tubulin detyrosination

6JZC の概要

• エントリーDOI: 10.2210/pdb6jzc/pdb
• 分子名称: Tubulinyl-Tyr carboxypeptidase 2, Small vasohibin-binding protein, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: vash2, svbp, tubulin detyrosination, cytosolic protein
• 由来する生物種: Mus musculus (Mouse); 詳細
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 102569.80

構造登録者

Chen, Z.,Ling, Y.,Zeyuan, G.,Zhu, L. (登録日: 2019-05-01, 公開日: 2019-07-17, 最終更新日: 2024-03-27)

主引用文献

Zhou, C.,Yan, L.,Zhang, W.H.,Liu, Z.
Structural basis of tubulin detyrosination by VASH2/SVBP heterodimer.
Nat Commun, 10:3212-3212, 2019

PubMed Abstract: The C-terminus of α-tubulin undergoes a detyrosination/tyrosination cycle and dysregulation of this cycle is associated with cancer and other diseases. The molecular mechanisms of tubulin tyrosination are well studied, however it has remained unknown how tyrosine is cleaved from the tubulin tail. Here, we report the crystal structure of the long-sought detyrosination enzyme, the VASH2/SVBP heterodimer at 2.2 Å resolution and the structure of the tail/VASH2/SVBP complex at 2.5 Å resolution. VASH2 possesses a non-canonical Cys-His-Ser catalytic architecture for tyrosine cleavage. The dynamics of the α1- and α2- helices of VASH2 are related to the insolubility of VASH2. SVBP plays a chaperone-like role by extensively interacting with VASH2 and stabilizing these dynamic helices. A positively charged groove around the catalytic pocket and the α1- and α2- helices of VASH2 targets the tubulin tail for detyrosination. We provide insights into the mechanisms underlying the cycle of tubulin tyrosine cleavage and religation.

PubMed: 31324789
DOI: 10.1038/s41467-019-11277-8

実験手法

X-RAY DIFFRACTION (2.201 Å)