8F5O

Structure of Leishmania tarentolae IFT-A (state 1)

8F5O の概要

• エントリーDOI: 10.2210/pdb8f5o/pdb
• EMDBエントリー: 28866
• 分子名称: Intraflagellar transport protein 122B, putative, Intraflagellar transport protein 122 homolog, WD_REPEATS_REGION domain-containing protein, ... (7 entities in total)
• 機能のキーワード: cilia, ift, protein transport
• 由来する生物種: Leishmania tarentolae; 詳細
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 839002.27

構造登録者

Zhou, H.,Brown, A. (登録日: 2022-11-14, 公開日: 2022-12-21, 最終更新日: 2024-05-22)

主引用文献

Meleppattu, S.,Zhou, H.,Dai, J.,Gui, M.,Brown, A.
Mechanism of IFT-A polymerization into trains for ciliary transport.
Cell, 185:4986-, 2022

PubMed Abstract: Intraflagellar transport (IFT) is the highly conserved process by which proteins are transported along ciliary microtubules by a train-like polymeric assembly of IFT-A and IFT-B complexes. IFT-A is sandwiched between IFT-B and the ciliary membrane, consistent with its putative role in transporting transmembrane and membrane-associated cargoes. Here, we have used single-particle analysis electron cryomicroscopy (cryo-EM) to determine structures of native IFT-A complexes. We show that subcomplex rearrangements enable IFT-A to polymerize laterally on anterograde IFT trains, revealing a cooperative assembly mechanism. Surprisingly, we discover that binding of IFT-A to IFT-B shields the preferred lipid-binding interface from the ciliary membrane but orients an interconnected network of β-propeller domains with the capacity to accommodate diverse cargoes toward the ciliary membrane. This work provides a mechanistic basis for understanding IFT-train assembly and cargo interactions.

PubMed: 36563665
DOI: 10.1016/j.cell.2022.11.033

実験手法

ELECTRON MICROSCOPY (3.5 Å)