+検索条件
-Structure paper
タイトル | Malaria parasite translocon structure and mechanism of effector export. |
---|---|
ジャーナル・号・ページ | Nature, Vol. 561, Issue 7721, Page 70-75, Year 2018 |
掲載日 | 2018年8月27日 |
著者 | Chi-Min Ho / Josh R Beck / Mason Lai / Yanxiang Cui / Daniel E Goldberg / Pascal F Egea / Z Hong Zhou / |
PubMed 要旨 | 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 ...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. |
リンク | Nature / PubMed:30150771 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 4.16 - 4.23 Å |
構造データ | |
化合物 | ChemComp-AGS: |
由来 |
|
キーワード | PROTEIN TRANSPORT / Translocon / Membrane Protein / ATPase |