6VE7
The inner junction complex of Chlamydomonas reinhardtii doublet microtubule
This is a non-PDB format compatible entry.
Summary for 6VE7
| Entry DOI | 10.2210/pdb6ve7/pdb |
| EMDB information | 20858 |
| Descriptor | Flagellar associated protein, MAGNESIUM ION, GUANOSINE-5'-DIPHOSPHATE, ... (12 entities in total) |
| Functional Keywords | cilia, doublet, axoneme, microtubule inner protein, structural protein |
| Biological source | Chlamydomonas reinhardtii More |
| Total number of polymer chains | 62 |
| Total formula weight | 2845886.26 |
| Authors | Khalifa, A.A.Z.,Ichikawa, M.,Bui, K.H. (deposition date: 2019-12-30, release date: 2020-02-05, Last modification date: 2024-10-09) |
| Primary citation | Khalifa, A.A.Z.,Ichikawa, M.,Dai, D.,Kubo, S.,Black, C.,Peri, K.,McAlear, T.S.,Veyron, S.,Yang, S.K.,Vargas, J.,Bechstedt, S.,Trempe, J.F.,Bui, K.H. The inner junction complex of the cilia is an interaction hub that involves tubulin post-translational modifications. Elife, 9:-, 2020 Cited by PubMed Abstract: Microtubules are cytoskeletal structures involved in stability, transport and organization in the cell. The building blocks, the α- and β-tubulin heterodimers, form protofilaments that associate laterally into the hollow microtubule. Microtubule also exists as highly stable doublet microtubules in the cilia where stability is needed for ciliary beating and function. The doublet microtubule maintains its stability through interactions at its inner and outer junctions where its A- and B-tubules meet. Here, using cryo-electron microscopy, bioinformatics and mass spectrometry of the doublets of and , we identified two new inner junction proteins, FAP276 and FAP106, and an inner junction-associated protein, FAP126, thus presenting the complete answer to the inner junction identity and localization. Our structural study of the doublets shows that the inner junction serves as an interaction hub that involves tubulin post-translational modifications. These interactions contribute to the stability of the doublet and hence, normal ciliary motility. PubMed: 31951202DOI: 10.7554/eLife.52760 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.6 Å) |
Structure validation
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