4YLS

Tubulin Glutamylase

4YLS の概要

• エントリーDOI: 10.2210/pdb4yls/pdb
• 関連するPDBエントリー: 4YLR
• 分子名称: Tubulin polyglutamylase TTLL7, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER (3 entities in total)
• 機能のキーワード: enzyme, ligase
• 由来する生物種: Homo sapiens (Human)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 57772.91

構造登録者

Garnham, C.P.,Vemu, A.,Wilson-Kubalek, E.M.,Yu, I.,Szyk, A.,Lander, G.C.,Milligan, R.A.,Roll-Mecak, A. (登録日: 2015-03-05, 公開日: 2015-06-17, 最終更新日: 2024-02-28)

主引用文献

Garnham, C.P.,Vemu, A.,Wilson-Kubalek, E.M.,Yu, I.,Szyk, A.,Lander, G.C.,Milligan, R.A.,Roll-Mecak, A.
Multivalent Microtubule Recognition by Tubulin Tyrosine Ligase-like Family Glutamylases.
Cell, 161:1112-1123, 2015

PubMed Abstract: Glutamylation, the most prevalent tubulin posttranslational modification, marks stable microtubules and regulates recruitment and activity of microtubule- interacting proteins. Nine enzymes of the tubulin tyrosine ligase-like (TTLL) family catalyze glutamylation. TTLL7, the most abundant neuronal glutamylase, adds glutamates preferentially to the β-tubulin tail. Coupled with ensemble and single-molecule biochemistry, our hybrid X-ray and cryo-electron microscopy structure of TTLL7 bound to the microtubule delineates a tripartite microtubule recognition strategy. The enzyme uses its core to engage the disordered anionic tails of α- and β-tubulin, and a flexible cationic domain to bind the microtubule and position itself for β-tail modification. Furthermore, we demonstrate that all single-chain TTLLs with known glutamylase activity utilize a cationic microtubule-binding domain analogous to that of TTLL7. Therefore, our work reveals the combined use of folded and intrinsically disordered substrate recognition elements as the molecular basis for specificity among the enzymes primarily responsible for chemically diversifying cellular microtubules.

PubMed: 25959773
DOI: 10.1016/j.cell.2015.04.003

実験手法

X-RAY DIFFRACTION (2.6 Å)