9OT2

13PF microtubule symmetry expansion

9OT2 の概要

• エントリーDOI: 10.2210/pdb9ot2/pdb
• EMDBエントリー: 70819
• 分子名称: Tubulin alpha-1B chain, Tubulin beta chain, GUANOSINE-5'-TRIPHOSPHATE, ... (6 entities in total)
• 機能のキーワード: microtubule, spef1, cilia, structural protein
• 由来する生物種: Bos taurus (domestic cattle); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 102002.83

構造登録者

Bui, K.H.,Legal, T.L. (登録日: 2025-05-26, 公開日: 2025-07-30)

主引用文献

Legal, T.,Joachimiak, E.,Parra, M.,Peng, W.,Tam, A.,Black, C.,Guha, M.,Nguyen, C.A.,Ghanaeian, A.,Valente-Paterno, M.,Brouhard, G.,Gaertig, J.,Wloga, D.,Bui, K.H.
Structure of the ciliary tip central pair reveals the unique role of the microtubule-seam binding protein SPEF1.
Curr.Biol., 35:3404-3417.e6, 2025

PubMed Abstract: Motile cilia are unique organelles with the ability to move autonomously. The force generated by beating cilia propels cells and moves fluids. The ciliary skeleton is made of peripheral doublet microtubules and a central pair (CP) with a distinct structure at the tip. In this study, we present a high-resolution structure of the CP in the ciliary tip of the ciliate Tetrahymena thermophila and identify several tip proteins that bind and form unique patterns on both microtubules of the tip CP. Two of those proteins that contain tubulin polymerization-promoting protein (TPPP)-like domains, TLP1 and TLP2, bind to high curvature regions of the microtubule. TLP2, which contains two TPPP-like domains, is an unusually long protein that wraps laterally around half a microtubule and forms the bridge between the two microtubules. Moreover, we found that the conserved protein SPEF1 binds to both microtubule seams and crosslinked the two microtubules. In vitro, human SPEF1 binds to the microtubule seam as visualized by cryoelectron tomography and subtomogram averaging. Single-molecule microtubule dynamics assays indicate that SPEF1 stabilizes microtubules in vitro. Together, these data show that the proteins in the tip CP maintain stable microtubule structures and play important roles in maintaining the integrity of the axoneme.

PubMed: 40651469
DOI: 10.1016/j.cub.2025.06.020

実験手法

ELECTRON MICROSCOPY (5.8 Å)