8BDA

IFTA complex in anterograde intraflagellar transport trains (Chlamydomonas reinhardtii)

これはPDB形式変換不可エントリーです。

8BDA の概要

• エントリーDOI: 10.2210/pdb8bda/pdb
• 関連するPDBエントリー: 8BD7
• EMDBエントリー: 15977 15978 15979 15980
• 分子名称: Intraflagellar transport protein 121, Intraflagellar transport protein 139, Intraflagellar transport particle protein 140, ... (5 entities in total)
• 機能のキーワード: cilia, ift, intraflagellar, transport, protein transport
• 由来する生物種: Chlamydomonas reinhardtii; 詳細
• タンパク質・核酸の鎖数: 5
• 化学式量合計: 736277.45

構造登録者

Lacey, S.E.,Foster, H.E.,Pigino, G. (登録日: 2022-10-18, 公開日: 2023-01-11, 最終更新日: 2024-07-24)

主引用文献

Lacey, S.E.,Foster, H.E.,Pigino, G.
The molecular structure of IFT-A and IFT-B in anterograde intraflagellar transport trains.
Nat.Struct.Mol.Biol., 30:584-593, 2023

PubMed Abstract: Anterograde intraflagellar transport (IFT) trains are essential for cilia assembly and maintenance. These trains are formed of 22 IFT-A and IFT-B proteins that link structural and signaling cargos to microtubule motors for import into cilia. It remains unknown how the IFT-A/-B proteins are arranged into complexes and how these complexes polymerize into functional trains. Here we use in situ cryo-electron tomography of Chlamydomonas reinhardtii cilia and AlphaFold2 protein structure predictions to generate a molecular model of the entire anterograde train. We show how the conformations of both IFT-A and IFT-B are dependent on lateral interactions with neighboring repeats, suggesting that polymerization is required to cooperatively stabilize the complexes. Following three-dimensional classification, we reveal how IFT-B extends two flexible tethers to maintain a connection with IFT-A that can withstand the mechanical stresses present in actively beating cilia. Overall, our findings provide a framework for understanding the fundamental processes that govern cilia assembly.

PubMed: 36593313
DOI: 10.1038/s41594-022-00905-5

実験手法

ELECTRON MICROSCOPY (20.7 Å)