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TitleStructural basis for microtubule binding and release by dynein.
Journal, issue, pagesScience, Vol. 337, Issue 6101, Page 1532-1536, Year 2012
Publish dateSep 21, 2012
AuthorsW B Redwine / R Hernandez-Lopez / S Zou / J Huang / S L Reck-Peterson / A E Leschziner /
PubMed AbstractCytoplasmic 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- ...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 ~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.
External linksScience / PubMed:22997337 / PubMed Central
MethodsEM (helical sym.)
Resolution9.7 Å
Structure data

5439

3j1t

3j1u

EMDB-5439: Structural basis for microtubule binding and release by dynein
PDB-3j1t: High affinity dynein microtubule binding domain - tubulin complex
PDB-3j1u: Low affinity dynein microtubule binding domain - tubulin complex
Method: EM (helical sym.) / Resolution: 9.7 Å

Source
  • mus musculus (house mouse)
  • bos taurus (cattle)
KeywordsMOTOR PROTEIN/STRUCTURAL PROTEIN / MOTOR PROTEIN-STRUCTURAL PROTEIN complex

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