3JAO

Ciliary microtubule doublet

3JAO の概要

• エントリーDOI: 10.2210/pdb3jao/pdb
• EMDBエントリー: 6312
• 分子名称: Tubulin alpha 1A chain, Tubulin beta chain, GUANOSINE-5'-TRIPHOSPHATE, ... (6 entities in total)
• 機能のキーワード: tubulin, microtubule doublet, cilia, structural protein
• 由来する生物種: Tetrahymena thermophila; 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 101108.01

構造登録者

Maheshwari, A.,Obbineni, J.M.,Bui, K.H.,Shibata, K.,Toyoshima, Y.Y.,Ishikawa, T. (登録日: 2015-06-18, 公開日: 2015-08-05, 最終更新日: 2024-02-21)

主引用文献

Maheshwari, A.,Obbineni, J.M.,Bui, K.H.,Shibata, K.,Toyoshima, Y.Y.,Ishikawa, T.
alpha- and beta-Tubulin Lattice of the Axonemal Microtubule Doublet and Binding Proteins Revealed by Single Particle Cryo-Electron Microscopy and Tomography.
Structure, 23:1584-1595, 2015

PubMed Abstract: Microtubule doublet (MTD) is the main skeleton of cilia/flagella. Many proteins, such as dyneins and radial spokes, bind to MTD, and generate or regulate force. While the structure of the reconstituted microtubule has been solved at atomic resolution, nature of the axonemal MTD is still unclear. There are a few hypotheses of the lattice arrangement of its α- and β-tubulins, but it has not been described how dyneins and radial spokes bind to MTD. In this study, we analyzed the three-dimensional structure of Tetrahymena MTD at ∼19 Å resolution by single particle cryo-electron microscopy. To identify α- and β-tubulins, we combined image analysis of MTD with specific kinesin decoration. This work reveals that α- and β-tubulins form a B-lattice arrangement in the entire MTD with a seam at the outer junction. We revealed the unique way in which inner arm dyneins, radial spokes, and proteins inside MTD bind and bridge protofilaments.

PubMed: 26211611
DOI: 10.1016/j.str.2015.06.017

実験手法

ELECTRON MICROSCOPY (23 Å)