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-Structure paper
Title | Remodeling and activation mechanisms of outer arm dyneins revealed by cryo-EM. |
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Journal, issue, pages | EMBO Rep, Vol. 22, Issue 9, Page e52911, Year 2021 |
Publish date | Sep 6, 2021 |
Authors | Shintaroh Kubo / Shun Kai Yang / Corbin S Black / Daniel Dai / Melissa Valente-Paterno / Jacek Gaertig / Muneyoshi Ichikawa / Khanh Huy Bui / |
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 ...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. |
External links | EMBO Rep / PubMed:34338432 / PubMed Central |
Methods | EM (single particle) |
Resolution | 8.0 Å |
Structure data | EMDB-23926, PDB-7moq: |
Chemicals | ChemComp-ADP: ChemComp-ATP: ChemComp-GDP: ChemComp-GTP: ChemComp-MG: |
Source |
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Keywords | STRUCTURAL PROTEIN / cilia / doublet / axoneme / outer dynein arm / dynein |