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TitleStructure of a microtubule-bound axonemal dynein.
Journal, issue, pagesNat Commun, Vol. 12, Issue 1, Page 477, Year 2021
Publish dateJan 20, 2021
AuthorsTravis Walton / Hao Wu / Alan Brown /
PubMed AbstractAxonemal 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 ...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.
External linksNat Commun / PubMed:33473120 / PubMed Central
MethodsEM (helical sym.)
Resolution3.3 - 7.5 Å
Structure data

EMDB-23082, PDB-7kzm:
Outer dynein arm bound to doublet microtubules from C. reinhardtii
Method: EM (helical sym.) / Resolution: 7.5 Å

EMDB-23083, PDB-7kzn:
Outer dynein arm core subcomplex from C. reinhardtii
Method: EM (helical sym.) / Resolution: 4.0 Å

EMDB-23084, PDB-7kzo:
Outer dynein arm docking complex bound to doublet microtubules from C. reinhardtii
Method: EM (helical sym.) / Resolution: 3.3 Å

Chemicals

ChemComp-GTP:
GUANOSINE-5'-TRIPHOSPHATE / GTP, energy-carrying molecule*YM / Guanosine triphosphate

ChemComp-MG:
Unknown entry

ChemComp-GDP:
GUANOSINE-5'-DIPHOSPHATE / GDP, energy-carrying molecule*YM / Guanosine diphosphate

Source
  • chlamydomonas reinhardtii (plant)
KeywordsMOTOR PROTEIN / dynein / microtubule / cilia

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