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Dyneins power microtubule motility using ringshaped, AAA-containing motor domains. Here, we report X-ray and electron microscopy (EM) structures of yeast dynein bound to different ATP analogs, which collectively provide insight into the roles of dynein's two major ATPase sites, AAA1 and AAA3, in the conformational change mechanism. ATP binding to AAA1 triggers a cascade of conformational changes that propagate to all six AAA domains and cause a large movement of the "linker," dynein'sdoi:10.1016/j.cell.2014.10.018 pmid:25417161 pmcid:PMC4269335 fatcat:wje4as5bznea7n4glscrypnqvy