7KZO

Outer dynein arm docking complex bound to doublet microtubules from C. reinhardtii

This is a non-PDB format compatible entry.

Summary for 7KZO

• Entry DOI: 10.2210/pdb7kzo/pdb
• EMDB information: 23084
• Descriptor: Tubulin beta, Tubulin alpha, Dynein gamma chain, flagellar outer arm, ... (9 entities in total)
• Functional Keywords: dynein, microtubule, cilia, motor protein
• Biological source: Chlamydomonas reinhardtii; More
• Total number of polymer chains: 20
• Total formula weight: 1529016.21

Authors

Walton, T.,Wu, H.,Brown, A.B. (deposition date: 2020-12-10, release date: 2021-01-20, Last modification date: 2024-03-06)

Primary citation

Walton, T.,Wu, H.,Brown, A.
Structure of a microtubule-bound axonemal dynein.
Nat Commun, 12:477-477, 2021

PubMed Abstract: Axonemal dyneins are tethered to doublet microtubules inside cilia to drive ciliary beating, a process critical for cellular motility and extracellular fluid flow. Axonemal dyneins are evolutionarily and biochemically distinct from cytoplasmic dyneins that transport cargo, and the mechanisms regulating their localization and function are poorly understood. Here, we report a single-particle cryo-EM reconstruction of a three-headed axonemal dynein natively bound to doublet microtubules isolated from cilia. The slanted conformation of the axonemal dynein causes interaction of its motor domains with the neighboring dynein complex. Our structure shows how a heterotrimeric docking complex specifically localizes the linear array of axonemal dyneins to the doublet microtubule by directly interacting with the heavy chains. Our structural analysis establishes the arrangement of conserved heavy, intermediate and light chain subunits, and provides a framework to understand the roles of individual subunits and the interactions between dyneins during ciliary waveform generation.

PubMed: 33473120
DOI: 10.1038/s41467-020-20735-7

Experimental method

ELECTRON MICROSCOPY (3.3 Å)