5OWO
Human cytoplasmic Dynein N-Terminus dimerization domain at 1.8 Angstrom resolution
Summary for 5OWO
| Entry DOI | 10.2210/pdb5owo/pdb |
| Descriptor | Cytoplasmic dynein 1 heavy chain 1, GLYCEROL, MAGNESIUM ION, ... (7 entities in total) |
| Functional Keywords | dynein, heavy chain, dimerization domain, motor protein |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 4 |
| Total formula weight | 90191.91 |
| Authors | Urnavicius, L.,Lau, C.K.,Elshenawy, M.M.,Morales-Rios, E.,Motz, C.,Yildiz, A.,Carter, A.P. (deposition date: 2017-09-01, release date: 2018-07-11, Last modification date: 2024-10-16) |
| Primary citation | Urnavicius, L.,Lau, C.K.,Elshenawy, M.M.,Morales-Rios, E.,Motz, C.,Yildiz, A.,Carter, A.P. Cryo-EM shows how dynactin recruits two dyneins for faster movement. Nature, 554:202-206, 2018 Cited by PubMed Abstract: Dynein and its cofactor dynactin form a highly processive microtubule motor in the presence of an activating adaptor, such as BICD2. Different adaptors link dynein and dynactin to distinct cargoes. Here we use electron microscopy and single-molecule studies to show that adaptors can recruit a second dynein to dynactin. Whereas BICD2 is biased towards recruiting a single dynein, the adaptors BICDR1 and HOOK3 predominantly recruit two dyneins. We find that the shift towards a double dynein complex increases both the force and speed of the microtubule motor. Our 3.5 Å resolution cryo-electron microscopy reconstruction of a dynein tail-dynactin-BICDR1 complex reveals how dynactin can act as a scaffold to coordinate two dyneins side-by-side. Our work provides a structural basis for understanding how diverse adaptors recruit different numbers of dyneins and regulate the motile properties of the dynein-dynactin transport machine. PubMed: 29420470DOI: 10.1038/nature25462 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.79 Å) |
Structure validation
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