6WSL

Cryo-EM structure of VASH1-SVBP bound to microtubules

6WSL の概要

• エントリーDOI: 10.2210/pdb6wsl/pdb
• EMDBエントリー: 21893
• 分子名称: Tubulin alpha-1A chain, Tubulin beta-3 chain, Tubulinyl-Tyr carboxypeptidase 1, ... (6 entities in total)
• 機能のキーワード: microtubule, posttranslational modification, detyrosination, vasohibin, protein binding
• 由来する生物種: Homo sapiens (Human); 詳細
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 278633.47

構造登録者

Li, F.,Li, Y.,Yu, H. (登録日: 2020-05-01, 公開日: 2020-08-26, 最終更新日: 2024-03-06)

主引用文献

Li, F.,Li, Y.,Ye, X.,Gao, H.,Shi, Z.,Luo, X.,Rice, L.M.,Yu, H.
Cryo-EM structure of VASH1-SVBP bound to microtubules.
Elife, 9:-, 2020

PubMed Abstract: The dynamic tyrosination-detyrosination cycle of α-tubulin regulates microtubule functions. Perturbation of this cycle impairs mitosis, neural physiology, and cardiomyocyte contraction. The carboxypeptidases vasohibins 1 and 2 (VASH1 and VASH2), in complex with the small vasohibin-binding protein (SVBP), mediate α-tubulin detyrosination. These enzymes detyrosinate microtubules more efficiently than soluble αβ-tubulin heterodimers. The structural basis for this substrate preference is not understood. Using cryo-electron microscopy (cryo-EM), we have determined the structure of human VASH1-SVBP bound to microtubules. The acidic C-terminal tail of α-tubulin binds to a positively charged groove near the active site of VASH1. VASH1 forms multiple additional contacts with the globular domain of α-tubulin, including contacts with a second α-tubulin in an adjacent protofilament. Simultaneous engagement of two protofilaments by VASH1 can only occur within the microtubule lattice, but not with free αβ heterodimers. These lattice-specific interactions enable preferential detyrosination of microtubules by VASH1.

PubMed: 32773040
DOI: 10.7554/eLife.58157

実験手法

ELECTRON MICROSCOPY (3.1 Å)