Summary for 6U42
| Entry DOI | 10.2210/pdb6u42/pdb |
| EMDB information | 20631 20632 20633 20634 20635 20636 20637 |
| Descriptor | Tubulin beta, FAP45, RIB30, ... (41 entities in total) |
| Functional Keywords | motile cilia, microtubule doublet, repetitive structure, protein fibril |
| Biological source | Chlamydomonas reinhardtii More |
| Total number of polymer chains | 451 |
| Total formula weight | 21385503.05 |
| Authors | Ma, M.,Stoyanova, M.,Rademacher, G.,Dutcher, S.K.,Brown, A.,Zhang, R. (deposition date: 2019-08-22, release date: 2019-11-13, Last modification date: 2024-10-23) |
| Primary citation | Ma, M.,Stoyanova, M.,Rademacher, G.,Dutcher, S.K.,Brown, A.,Zhang, R. Structure of the Decorated Ciliary Doublet Microtubule. Cell, 179:909-922.e12, 2019 Cited by PubMed Abstract: The axoneme of motile cilia is the largest macromolecular machine of eukaryotic cells. In humans, impaired axoneme function causes a range of ciliopathies. Axoneme assembly, structure, and motility require a radially arranged set of doublet microtubules, each decorated in repeating patterns with non-tubulin components. We use single-particle cryo-electron microscopy to visualize and build an atomic model of the repeating structure of a native axonemal doublet microtubule, which reveals the identities, positions, repeat lengths, and interactions of 38 associated proteins, including 33 microtubule inner proteins (MIPs). The structure demonstrates how these proteins establish the unique architecture of doublet microtubules, maintain coherent periodicities along the axoneme, and stabilize the microtubules against the repeated mechanical stress induced by ciliary motility. Our work elucidates the architectural principles that underpin the assembly of this large, repetitive eukaryotic structure and provides a molecular basis for understanding the etiology of human ciliopathies. PubMed: 31668805DOI: 10.1016/j.cell.2019.09.030 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.4 Å) |
Structure validation
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