6ZYW
Outer Dynein Arm-Shulin complex - overall structure (Tetrahymena thermophila)
Summary for 6ZYW
| Entry DOI | 10.2210/pdb6zyw/pdb |
| EMDB information | 11576 |
| Descriptor | Dynein-1-alpha heavy chain, flagellar inner arm I1 complex protein, putative, Dynein light chain, Dynein light chain 2A, ... (20 entities in total) |
| Functional Keywords | cilia, dynein, microtubules, motor, motor protein |
| Biological source | Tetrahymena thermophila SB210 More |
| Total number of polymer chains | 19 |
| Total formula weight | 2130902.11 |
| Authors | Mali, G.R.,Abid Ali, F.,Lau, C.K.,Carter, A.P. (deposition date: 2020-08-03, release date: 2021-01-20, Last modification date: 2024-05-01) |
| Primary citation | Mali, G.R.,Ali, F.A.,Lau, C.K.,Begum, F.,Boulanger, J.,Howe, J.D.,Chen, Z.A.,Rappsilber, J.,Skehel, M.,Carter, A.P. Shulin packages axonemal outer dynein arms for ciliary targeting. Science, 371:910-916, 2021 Cited by PubMed Abstract: The main force generators in eukaryotic cilia and flagella are axonemal outer dynein arms (ODAs). During ciliogenesis, these ~1.8-megadalton complexes are assembled in the cytoplasm and targeted to cilia by an unknown mechanism. Here, we used the ciliate to identify two factors (Q22YU3 and Q22MS1) that bind ODAs in the cytoplasm and are required for ODA delivery to cilia. Q22YU3, which we named Shulin, locked the ODA motor domains into a closed conformation and inhibited motor activity. Cryo-electron microscopy revealed how Shulin stabilized this compact form of ODAs by binding to the dynein tails. Our findings provide a molecular explanation for how newly assembled dyneins are packaged for delivery to the cilia. PubMed: 33632841DOI: 10.1126/science.abe0526 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (8.78 Å) |
Structure validation
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