4AKI

Dynein Motor Domain - LuAc derivative

4AKI の概要

• エントリーDOI: 10.2210/pdb4aki/pdb
• 関連するPDBエントリー: 1B8X 1DUG 1GNE 1GTA 1GTB 1M99 1M9A 1M9B 1U87 1U88 1UA5 1Y6E 4AI6 4AKG 4AKH
• 分子名称: GLUTATHIONE S-TRANSFERASE CLASS-MU 26 KDA ISOZYME, DYNEIN HEAVY CHAIN CYTOPLASMIC, ADENOSINE-5'-TRIPHOSPHATE, SULFATE ION, ... (4 entities in total)
• 機能のキーワード: motor protein, dynein, dynein heavy chain, dynein motor domain, motor protein aaa+ protein, asce protein, p-loop ntpase, cytoskeletal motor
• 由来する生物種: SCHISTOSOMA JAPONICUM; 詳細
• 細胞内の位置: Cytoplasm, cytoskeleton : P36022
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 622049.60

構造登録者

Schmidt, H.,Gleave, E.S.,Carter, A.P. (登録日: 2012-02-22, 公開日: 2012-03-14, 最終更新日: 2024-05-08)

主引用文献

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

実験手法

X-RAY DIFFRACTION (3.7 Å)