Journal
SCIENCE
Volume 337, Issue 6101, Pages 1532-1536Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1224151
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Funding
- National Science Foundation [ECS-0335765]
- Rita Allen Foundation
- Harvard Armenise Foundation
- NIH [1 DP2 OD004268-1]
- Alfred P. Sloan Foundation
- Consejo Nacional de Ciencia y Tecnologia
- Fundacion Mexico en Harvard
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Cytoplasmic dynein is a microtubule-based motor required for intracellular transport and cell division. Its movement involves coupling cycles of track binding and release with cycles of force-generating nucleotide hydrolysis. How this is accomplished given the similar to 25 nanometers separating dynein's track- and nucleotide-binding sites is not understood. Here, we present a subnanometer-resolution structure of dynein's microtubule-binding domain bound to microtubules by cryo-electron microscopy that was used to generate a pseudo-atomic model of the complex with molecular dynamics. We identified large rearrangements triggered by track binding and specific interactions, confirmed by mutagenesis and single-molecule motility assays, which tune dynein's affinity for microtubules. Our results provide a molecular model for how dynein's binding to microtubules is communicated to the rest of the motor.
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