6E10

PTEX Core Complex in the Engaged (Extended) State

6E10 の概要

• エントリーDOI: 10.2210/pdb6e10/pdb
• EMDBエントリー: 8951 8952
• 分子名称: Heat shock protein 101, Exported protein 2, Translocon component PTEX150, ... (6 entities in total)
• 機能のキーワード: translocon, membrane protein, atpase, protein transport
• 由来する生物種: Plasmodium falciparum (isolate 3D7); 詳細
• タンパク質・核酸の鎖数: 28
• 化学式量合計: 1089917.20

構造登録者

Ho, C.,Lai, M.,Zhou, Z.H. (登録日: 2018-07-08, 公開日: 2018-08-22, 最終更新日: 2024-11-20)

主引用文献

Ho, C.M.,Beck, J.R.,Lai, M.,Cui, Y.,Goldberg, D.E.,Egea, P.F.,Zhou, Z.H.
Malaria parasite translocon structure and mechanism of effector export.
Nature, 561:70-75, 2018

PubMed Abstract: The putative Plasmodium translocon of exported proteins (PTEX) is essential for transport of malarial effector proteins across a parasite-encasing vacuolar membrane into host erythrocytes, but the mechanism of this process remains unknown. Here we show that PTEX is a bona fide translocon by determining structures of the PTEX core complex at near-atomic resolution using cryo-electron microscopy. We isolated the endogenous PTEX core complex containing EXP2, PTEX150 and HSP101 from Plasmodium falciparum in the 'engaged' and 'resetting' states of endogenous cargo translocation using epitope tags inserted using the CRISPR-Cas9 system. In the structures, EXP2 and PTEX150 interdigitate to form a static, funnel-shaped pseudo-seven-fold-symmetric protein-conducting channel spanning the vacuolar membrane. The spiral-shaped AAA+ HSP101 hexamer is tethered above this funnel, and undergoes pronounced compaction that allows three of six tyrosine-bearing pore loops lining the HSP101 channel to dissociate from the cargo, resetting the translocon for the next threading cycle. Our work reveals the mechanism of P. falciparum effector export, and will inform structure-based design of drugs targeting this unique translocon.

PubMed: 30150771
DOI: 10.1038/s41586-018-0469-4

実験手法

ELECTRON MICROSCOPY (4.16 Å)