6U0T
Protofilament Ribbon Flagellar Proteins Rib43a-S
6U0T の概要
エントリーDOI | 10.2210/pdb6u0t/pdb |
EMDBエントリー | 20602 |
分子名称 | Tubulin alpha chain, Tubulin beta chain, RIB43A protein, ... (6 entities in total) |
機能のキーワード | cilia, doublet, axoneme, microtubule inner protein, structural protein |
由来する生物種 | Tetrahymena thermophila 詳細 |
タンパク質・核酸の鎖数 | 13 |
化学式量合計 | 618805.80 |
構造登録者 | Ichikawa, M.,Khalifa, A.A.Z.,Vargas, J.,Basu, K.,Bui, K.H. (登録日: 2019-08-14, 公開日: 2019-09-25, 最終更新日: 2024-03-13) |
主引用文献 | 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 主引用文献が同じPDBエントリー |
実験手法 | ELECTRON MICROSCOPY (4.16 Å) |
構造検証レポート
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