7MOQ

The structure of the Tetrahymena thermophila outer dynein arm on doublet microtubule

This is a non-PDB format compatible entry.

Summary for 7MOQ

• Entry DOI: 10.2210/pdb7moq/pdb
• EMDB information: 23926
• Descriptor: Dynein-1-alpha heavy chain, flagellar inner arm I1 complex protein, putative, Dynein light chain, Dynein light chain 2A, ... (27 entities in total)
• Functional Keywords: cilia, doublet, axoneme, outer dynein arm, dynein, structural protein
• Biological source: Tetrahymena thermophila CU428; More
• Total number of polymer chains: 35
• Total formula weight: 2783901.16

Authors

Kubo, S.,Yang, S.K.,Ichikawa, M.,Bui, K.H. (deposition date: 2021-05-03, release date: 2021-07-14, Last modification date: 2024-05-29)

Primary citation

Kubo, S.,Yang, S.K.,Black, C.S.,Dai, D.,Valente-Paterno, M.,Gaertig, J.,Ichikawa, M.,Bui, K.H.
Remodeling and activation mechanisms of outer arm dyneins revealed by cryo-EM.
Embo Rep., 22:e52911-e52911, 2021

PubMed Abstract: Cilia are thin microtubule-based protrusions of eukaryotic cells. The swimming of ciliated protists and sperm cells is propelled by the beating of cilia. Cilia propagate the flow of mucus in the trachea and protect the human body from viral infections. The main force generators of ciliary beating are the outer dynein arms (ODAs) which attach to the doublet microtubules. The bending of cilia is driven by the ODAs' conformational changes caused by ATP hydrolysis. Here, we report the native ODA complex structure attaching to the doublet microtubule by cryo-electron microscopy. The structure reveals how the ODA complex is attached to the doublet microtubule via the docking complex in its native state. Combined with coarse-grained molecular dynamic simulations, we present a model of how the attachment of the ODA to the doublet microtubule induces remodeling and activation of the ODA complex.

PubMed: 34338432
DOI: 10.15252/embr.202152911

Experimental method

ELECTRON MICROSCOPY (8 Å)