9E5C

Cryo-EM structure of 96 nm repeat of microtubule doublet from T. brucei flagellum

これはPDB形式変換不可エントリーです。

9E5C の概要

• エントリーDOI: 10.2210/pdb9e5c/pdb
• EMDBエントリー: 47524
• 分子名称: EF-hand domain-containing family member C2, LIM zinc-binding domain-containing protein, Dynein heavy chain, putative, ... (160 entities in total)
• 機能のキーワード: flagella, microtubule, motor protein
• 由来する生物種: Trypanosoma brucei brucei TREU927; 詳細
• タンパク質・核酸の鎖数: 1166
• 化学式量合計: 63727105.21

構造登録者

Xia, X.,Shimogawa, M.M.,Wang, H.,Liu, S.,Wijono, A.,Langousis, G.,Kassem, A.M.,Wohlschlegel, J.A.,Hill, K.,Zhou, Z.H. (登録日: 2024-10-28, 公開日: 2025-03-12, 最終更新日: 2025-03-26)

主引用文献

Xia, X.,Shimogawa, M.M.,Wang, H.,Liu, S.,Wijono, A.,Langousis, G.,Kassem, A.M.,Wohlschlegel, J.A.,Hill, K.L.,Zhou, Z.H.
Trypanosome doublet microtubule structures reveal flagellum assembly and motility mechanisms.
Science, 387:eadr3314-eadr3314, 2025

PubMed Abstract: The flagellum of drives the parasite's characteristic screw-like motion and is essential for its replication, transmission, and pathogenesis. However, the molecular details of this process remain unclear. Here, we present high-resolution (up to 2.8 angstrom) cryo-electron microscopy structures of flagellar doublet microtubules (DMTs). Integrated modeling identified 154 different axonemal proteins inside and outside the DMT and, together with genetic and proteomic interrogation, revealed conserved and trypanosome-specific foundations of flagellum assembly and motility. We captured axonemal dynein motors in their pre-power stroke state. Comparing atomic models between pre- and post-power strokes defined how dynein structural changes drive sliding of adjacent DMTs during flagellar beating. This study illuminates structural dynamics underlying flagellar motility and identifies pathogen-specific proteins to consider for therapeutic interventions targeting neglected diseases.

PubMed: 40080582
DOI: 10.1126/science.adr3314

実験手法

ELECTRON MICROSCOPY (3.2 Å)