Insights into dynein motor domain function from a 3.3-Å crystal structure

Nat Struct Mol Biol. 2012 Mar 14;19(5):492-7, S1. doi: 10.1038/nsmb.2272.


Dyneins power the beating of cilia and flagella, transport various intracellular cargos and are necessary for mitosis. All dyneins have a ∼300-kDa motor domain consisting of a ring of six AAA+ domains. ATP hydrolysis in the AAA+ ring drives the cyclic relocation of a motile element, the linker domain, to generate the force necessary for movement. How the linker interacts with the ring during the ATP hydrolysis cycle is not known. Here we present a 3.3-Å crystal structure of the motor domain of Saccharomyces cerevisiae cytoplasmic dynein, crystallized in the absence of nucleotides. The linker is docked to a conserved site on AAA5, which is confirmed by mutagenesis as functionally necessary. Nucleotide soaking experiments show that the main ATP hydrolysis site in dynein (AAA1) is in a low-nucleotide affinity conformation and reveal the nucleotide interactions of the other three sites (AAA2, AAA3 and AAA4).

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Binding Sites
  • Crystallography, X-Ray
  • Dyneins / chemistry*
  • Dyneins / metabolism
  • Fungal Proteins / chemistry*
  • Fungal Proteins / metabolism
  • Models, Molecular
  • Nucleotides / metabolism
  • Protein Structure, Tertiary
  • Saccharomyces cerevisiae / chemistry*
  • Saccharomyces cerevisiae / metabolism


  • Fungal Proteins
  • Nucleotides
  • Dyneins

Associated data

  • PDB/4AI6
  • PDB/4AKG
  • PDB/4AKH
  • PDB/4AKI