|4ai6, resolution 3.40Å ()|
|Sites:||, , , , , , , , and|
|Ligands:||, , ,|
|Related:||1b8x, 1dug, 1gne, 1gta, 1gtb, 1m99, 1m9a, 1m9b, 1u87, 1u88, 1ua5, 1y6e, 4akg, 4akh, 4aki|
Dynein Motor Domain - ADP complex
Dyneins power the beating of cilia and flagella, transport various intracellular cargos and are necessary for mitosis. All dyneins have a approximately 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-A 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).
Insights into dynein motor domain function from a 3.3-A crystal structure., Schmidt H, Gleave ES, Carter AP, Nat Struct Mol Biol. 2012 Mar 14;19(5):492-7. doi: 10.1038/nsmb.2272. PMID:22426545
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.