+検索条件
-Structure paper
タイトル | Structural basis for microtubule binding and release by dynein. |
---|---|
ジャーナル・号・ページ | Science, Vol. 337, Issue 6101, Page 1532-1536, Year 2012 |
掲載日 | 2012年9月21日 |
著者 | W B Redwine / R Hernandez-Lopez / S Zou / J Huang / S L Reck-Peterson / A E Leschziner / |
PubMed 要旨 | 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- ...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. |
リンク | Science / PubMed:22997337 / PubMed Central |
手法 | EM (らせん対称) |
解像度 | 9.7 Å |
構造データ | |
由来 |
|
キーワード | MOTOR PROTEIN/STRUCTURAL PROTEIN (機関 (機械)) / MOTOR PROTEIN-STRUCTURAL PROTEIN complex (機関 (機械)) |