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• W2111004920 endingPage "497" @default.
• W2111004920 startingPage "492" @default.
• W2111004920 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)." @default.
• W2111004920 created "2016-06-24" @default.
• W2111004920 creator A5012194078 @default.
• W2111004920 creator A5050414435 @default.
• W2111004920 creator A5059994884 @default.
• W2111004920 date "2012-03-14" @default.
• W2111004920 modified "2023-09-27" @default.
• W2111004920 title "Insights into dynein motor domain function from a 3.3-Å crystal structure" @default.
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• W2111004920 doi "https://doi.org/10.1038/nsmb.2272" @default.
• W2111004920 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/3393637" @default.
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• W2111004920 hasPublicationYear "2012" @default.
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