Format

Send to

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

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

Author information

1
Medical Research Council Laboratory of Molecular Biology, Cambridge, UK.

Abstract

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).

PMID:
22426545
PMCID:
PMC3393637
DOI:
10.1038/nsmb.2272
[Indexed for MEDLINE]
Free PMC Article

Supplemental Content

Full text links

Icon for Nature Publishing Group Icon for PubMed Central
Loading ...
Support Center