7MIZ

Atomic structure of cortical microtubule from Toxoplasma gondii

これはPDB形式変換不可エントリーです。

7MIZ の概要

• エントリーDOI: 10.2210/pdb7miz/pdb
• EMDBエントリー: 23869 23870
• 分子名称: Microtubule associated protein SPM1, Tubulin alpha chain, Tubulin beta chain, ... (8 entities in total)
• 機能のキーワード: cortical, parasite, structural protein
• 由来する生物種: Toxoplasma gondii; 詳細
• タンパク質・核酸の鎖数: 100
• 化学式量合計: 4151024.13

構造登録者

Wang, X.,Brown, A.,Sibley, L.D.,Zhang, R. (登録日: 2021-04-18, 公開日: 2021-06-02, 最終更新日: 2024-10-23)

主引用文献

Wang, X.,Fu, Y.,Beatty, W.L.,Ma, M.,Brown, A.,David Sibley, L.,Zhang, R.
Cryo-EM structure of cortical microtubules from human parasite Toxoplasma gondii identifies their microtubule inner proteins.
Nat Commun, 12:3065-3065, 2021

PubMed Abstract: In living cells, microtubules (MTs) play pleiotropic roles, which require very different mechanical properties. Unlike the dynamic MTs found in the cytoplasm of metazoan cells, the specialized cortical MTs from Toxoplasma gondii, a prevalent human pathogen, are extraordinarily stable and resistant to detergent and cold treatments. Using single-particle cryo-EM, we determine their ex vivo structure and identify three proteins (TrxL1, TrxL2 and SPM1) as bona fide microtubule inner proteins (MIPs). These three MIPs form a mesh on the luminal surface and simultaneously stabilize the tubulin lattice in both longitudinal and lateral directions. Consistent with previous observations, deletion of the identified MIPs compromises MT stability and integrity under challenges by chemical treatments. We also visualize a small molecule like density at the Taxol-binding site of β-tubulin. Our results provide the structural basis to understand the stability of cortical MTs and suggest an evolutionarily conserved mechanism of MT stabilization from the inside.

PubMed: 34031406
DOI: 10.1038/s41467-021-23351-1

実験手法

ELECTRON MICROSCOPY (3.4 Å)