Ontology highlight
ABSTRACT:
SUBMITTER: Carter AP
PROVIDER: S-EPMC3169322 | biostudies-literature | 2011 Mar
REPOSITORIES: biostudies-literature
Carter Andrew P AP Cho Carol C Jin Lan L Vale Ronald D RD
Science (New York, N.Y.) 20110217 6021
Dyneins are microtubule-based motor proteins that power ciliary beating, transport intracellular cargos, and help to construct the mitotic spindle. Evolved from ring-shaped hexameric AAA-family adenosine triphosphatases (ATPases), dynein's large size and complexity have posed challenges for understanding its structure and mechanism. Here, we present a 6 angstrom crystal structure of a functional dimer of two ~300-kilodalton motor domains of yeast cytoplasmic dynein. The structure reveals an unus ...[more]