4AKG: Dynein Motor Domain - Atp 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).
PDB ID: 4AKGDownload
MMDB ID: 98032
PDB Deposition Date: 2012/2/22
Updated in MMDB: 2012/05
Experimental Method:
x-ray diffraction
Resolution: 3.3  Å
Similar Structures:
Biological Unit for 4AKG: dimeric; determined by author and by software (PISA)
Molecular Components in 4AKG
Label Count Molecule
Proteins (2 molecules)
Glutathione S-transferase Class-mu 26 KDA Isozyme, Dynein Heavy Chain Cytoplasmic(Gene symbol: DYN1)
Molecule annotation
Chemicals (10 molecules)
* Click molecule labels to explore molecular sequence information.

Citing MMDB