3JAO

Ciliary microtubule doublet

Summary for 3JAO

• Entry DOI: 10.2210/pdb3jao/pdb
• EMDB information: 6312
• Descriptor: Tubulin alpha 1A chain, Tubulin beta chain, GUANOSINE-5'-TRIPHOSPHATE, ... (6 entities in total)
• Functional Keywords: tubulin, microtubule doublet, cilia, structural protein
• Biological source: Tetrahymena thermophila; More
• Total number of polymer chains: 2
• Total formula weight: 101108.01

Authors

Maheshwari, A.,Obbineni, J.M.,Bui, K.H.,Shibata, K.,Toyoshima, Y.Y.,Ishikawa, T. (deposition date: 2015-06-18, release date: 2015-08-05, Last modification date: 2024-02-21)

Primary citation

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

Experimental method

ELECTRON MICROSCOPY (23 Å)