6U0T
Protofilament Ribbon Flagellar Proteins Rib43a-S
Summary for 6U0T
| Entry DOI | 10.2210/pdb6u0t/pdb |
| EMDB information | 20602 |
| Descriptor | Tubulin alpha chain, Tubulin beta chain, RIB43A protein, ... (6 entities in total) |
| Functional Keywords | cilia, doublet, axoneme, microtubule inner protein, structural protein |
| Biological source | Tetrahymena thermophila More |
| Total number of polymer chains | 13 |
| Total formula weight | 618805.80 |
| Authors | Ichikawa, M.,Khalifa, A.A.Z.,Vargas, J.,Basu, K.,Bui, K.H. (deposition date: 2019-08-14, release date: 2019-09-25, Last modification date: 2024-03-13) |
| Primary citation | Ichikawa, M.,Khalifa, A.A.Z.,Kubo, S.,Dai, D.,Basu, K.,Maghrebi, M.A.F.,Vargas, J.,Bui, K.H. Tubulin lattice in cilia is in a stressed form regulated by microtubule inner proteins. Proc.Natl.Acad.Sci.USA, 116:19930-19938, 2019 Cited by PubMed Abstract: Cilia, the hair-like protrusions that beat at high frequencies to propel a cell or move fluid around are composed of radially bundled doublet microtubules. In this study, we present a near-atomic resolution map of the doublet microtubule by cryoelectron microscopy. The map demonstrates that the network of microtubule inner proteins weaves into the tubulin lattice and forms an inner sheath. From mass spectrometry data and de novo modeling, we identified Rib43a proteins as the filamentous microtubule inner proteins in the protofilament ribbon region. The Rib43a-tubulin interaction leads to an elongated tubulin dimer distance every 2 dimers. In addition, the tubulin lattice structure with missing microtubule inner proteins (MIPs) by sarkosyl treatment shows significant longitudinal compaction and lateral angle change between protofilaments. These results are evidence that the MIPs directly affect and stabilize the tubulin lattice. It suggests that the doublet microtubule is an intrinsically stressed filament and that this stress could be manipulated in the regulation of ciliary waveforms. PubMed: 31527277DOI: 10.1073/pnas.1911119116 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (4.16 Å) |
Structure validation
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