Ontology highlight
ABSTRACT:
SUBMITTER: Bhabha G
PROVIDER: S-EPMC4269335 | biostudies-literature | 2014 Nov
REPOSITORIES: biostudies-literature
Bhabha Gira G Cheng Hui-Chun HC Zhang Nan N Moeller Arne A Liao Maofu M Speir Jeffrey A JA Cheng Yifan Y Vale Ronald D RD
Cell 20141101 4
Dyneins power microtubule motility using ring-shaped, 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's mechanica ...[more]