The 2.8 Å crystal structure of the dynein motor domain

Nature. 2012 Mar 7;484(7394):345-50. doi: 10.1038/nature10955.


Dyneins are microtubule-based AAA(+) motor complexes that power ciliary beating, cell division, cell migration and intracellular transport. Here we report the most complete structure obtained so far, to our knowledge, of the 380-kDa motor domain of Dictyostelium discoideum cytoplasmic dynein at 2.8 Å resolution; the data are reliable enough to discuss the structure and mechanism at the level of individual amino acid residues. Features that can be clearly visualized at this resolution include the coordination of ADP in each of four distinct nucleotide-binding sites in the ring-shaped AAA(+) ATPase unit, a newly identified interaction interface between the ring and mechanical linker, and junctional structures between the ring and microtubule-binding stalk, all of which should be critical for the mechanism of dynein motility. We also identify a long-range allosteric communication pathway between the primary ATPase and the microtubule-binding sites. Our work provides a framework for understanding the mechanism of dynein-based motility.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenosine Diphosphate / metabolism
  • Adenosine Triphosphate / metabolism
  • Allosteric Regulation
  • Binding Sites
  • Crystallography, X-Ray
  • Cytoplasmic Dyneins / chemistry*
  • Cytoplasmic Dyneins / metabolism
  • Dictyostelium / chemistry*
  • Hydrolysis
  • Microtubules / metabolism
  • Models, Biological
  • Models, Molecular
  • Movement
  • Protein Structure, Tertiary
  • Structure-Activity Relationship


  • Adenosine Diphosphate
  • Adenosine Triphosphate
  • Cytoplasmic Dyneins

Associated data

  • PDB/3VKG
  • PDB/3VKH