7RRO
Structure of the 48-nm repeat doublet microtubule from bovine tracheal cilia
This is a non-PDB format compatible entry.
Summary for 7RRO
| Entry DOI | 10.2210/pdb7rro/pdb |
| EMDB information | 24663 24664 |
| Descriptor | Protein C9orf135 homolog, Tektin-2, Uncharacterized protein C1orf189 homolog, ... (39 entities in total) |
| Functional Keywords | cilia, microtubule, dynein, motility, structural protein |
| Biological source | Bos taurus (Bovine) More |
| Total number of polymer chains | 429 |
| Total formula weight | 21608302.42 |
| Authors | Gui, M.,Anderson, J.R.,Botsch, J.J.,Meleppattu, S.,Singh, S.K.,Zhang, Q.,Brown, A. (deposition date: 2021-08-10, release date: 2021-10-27, Last modification date: 2024-06-05) |
| Primary citation | Gui, M.,Farley, H.,Anujan, P.,Anderson, J.R.,Maxwell, D.W.,Whitchurch, J.B.,Botsch, J.J.,Qiu, T.,Meleppattu, S.,Singh, S.K.,Zhang, Q.,Thompson, J.,Lucas, J.S.,Bingle, C.D.,Norris, D.P.,Roy, S.,Brown, A. De novo identification of mammalian ciliary motility proteins using cryo-EM. Cell, 184:5791-, 2021 Cited by PubMed Abstract: Dynein-decorated doublet microtubules (DMTs) are critical components of the oscillatory molecular machine of cilia, the axoneme, and have luminal surfaces patterned periodically by microtubule inner proteins (MIPs). Here we present an atomic model of the 48-nm repeat of a mammalian DMT, derived from a cryoelectron microscopy (cryo-EM) map of the complex isolated from bovine respiratory cilia. The structure uncovers principles of doublet microtubule organization and features specific to vertebrate cilia, including previously unknown MIPs, a luminal bundle of tektin filaments, and a pentameric dynein-docking complex. We identify a mechanism for bridging 48- to 24-nm periodicity across the microtubule wall and show that loss of the proteins involved causes defective ciliary motility and laterality abnormalities in zebrafish and mice. Our structure identifies candidate genes for diagnosis of ciliopathies and provides a framework to understand their functions in driving ciliary motility. PubMed: 34715025DOI: 10.1016/j.cell.2021.10.007 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.4 Å) |
Structure validation
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