4akg | pdb_00004akg

Dynein Motor Domain - ATP complex

spinqualitylabelsall models 4akg, resolution 3.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 4akg is a 2 chain structure with sequence from Schistosoma japonicum, saccharomyces cerevisiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: ADP, ATP, MG, SO4 Related: 1b8x, 1dug, 1gne, 1gta, 1gtb, 1m99, 1m9a, 1m9b, 1u87, 1u88, 1ua5, 1y6e, 4ai6, 4akh, 4aki Activity: Glutathione transferase, with EC number 2.5.1.18 Resources: FirstGlance, OCA, RCSB, PDBsum Publication Abstract from PubMed 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. See Also Dynein Glutathione S-transferase

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