Journal
SCIENCE
Volume 331, Issue 6021, Pages 1159-1165Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1202393
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Funding
- NIH
- Jane Coffin Child Foundation
- Lymphoma and Leukemia Foundation
- American Heart Association
- Genentech
- MRC [MC_UP_A025_1011] Funding Source: UKRI
- Medical Research Council [MC_UP_A025_1011] Funding Source: researchfish
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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 similar to 300-kilodalton motor domains of yeast cytoplasmic dynein. The structure reveals an unusual asymmetric arrangement of ATPase domains in the ring-shaped motor domain, the manner in which the mechanical element interacts with the ATPase ring, and an unexpected interaction between two coiled coils that create a base for the microtubule binding domain. The arrangement of these elements provides clues as to how adenosine triphosphate-driven conformational changes might be transmitted across the motor domain.
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