4AKH

Dynein Motor Domain - AMPPNP complex

Summary for 4AKH

• Entry DOI: 10.2210/pdb4akh/pdb
• Related: 1B8X 1DUG 1GNE 1GTA 1GTB 1M99 1M9A 1M9B 1U87 1U88 1UA5 1Y6E 4AI6 4AKG 4AKI
• Descriptor: GLUTATHIONE S-TRANSFERASE CLASS-MU 26 KDA ISOZYME, DYNEIN HEAVY CHAIN CYTOPLASMIC, ADENOSINE-5'-TRIPHOSPHATE, PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER, ... (5 entities in total)
• Functional Keywords: motor protein, motor protein-transferase complex, aaa+ protein, asce protein, motor protein p-loop ntpase, cytoskeletal motor
• Biological source: SCHISTOSOMA JAPONICUM; More
• Total number of polymer chains: 2
• Total formula weight: 622869.87

Authors

Schmidt, H.,Gleave, E.S.,Carter, A.P. (deposition date: 2012-02-22, release date: 2012-03-14, Last modification date: 2023-12-20)

Primary citation

Schmidt, H.,Gleave, E.S.,Carter, A.P.
Insights Into Dynein Motor Domain Function from a 3.3 Angstrom Crystal Structure
Nat.Struct.Mol.Biol., 19:492-, 2012

PubMed 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).

PubMed: 22426545
DOI: 10.1038/NSMB.2272

Experimental method

X-RAY DIFFRACTION (3.6 Å)