3JBP

Cryo-electron microscopy reconstruction of the Plasmodium falciparum 80S ribosome bound to E-tRNA

これはPDB形式変換不可エントリーです。

3JBP の概要

• エントリーDOI: 10.2210/pdb3jbp/pdb
• 関連するPDBエントリー: 3JBN 3JBO
• EMDBエントリー: 6452 6454 6456
• 分子名称: 18S ribosomal RNA, 40S ribosomal protein eS12, 40S ribosomal protein eS10, ... (78 entities in total)
• 機能のキーワード: ribosome
• 由来する生物種: Plasmodium falciparum 3D7; 詳細
• タンパク質・核酸の鎖数: 78
• 化学式量合計: 2888703.02

構造登録者

Sun, M.,Li, W.,Blomqvist, K.,Das, S.,Hashem, Y.,Dvorin, J.D.,Frank, J. (登録日: 2015-09-16, 公開日: 2015-10-14, 最終更新日: 2024-02-21)

主引用文献

Sun, M.,Li, W.,Blomqvist, K.,Das, S.,Hashem, Y.,Dvorin, J.D.,Frank, J.
Dynamical features of the Plasmodium falciparum ribosome during translation.
Nucleic Acids Res., 43:10515-10524, 2015

PubMed Abstract: Plasmodium falciparum, the mosquito-transmitted Apicomplexan parasite, causes the most severe form of human malaria. In the asexual blood-stage, the parasite resides within erythrocytes where it proliferates, multiplies and finally spreads to new erythrocytes. Development of drugs targeting the ribosome, the site of protein synthesis, requires specific knowledge of its structure and work cycle, and, critically, the ways they differ from those in the human host. Here, we present five cryo-electron microscopy (cryo-EM) reconstructions of ribosomes purified from P. falciparum blood-stage schizonts at sub-nanometer resolution. Atomic models were built from these density maps by flexible fitting. Significantly, our study has taken advantage of new capabilities of cryo-EM, in visualizing several structures co-existing in the sample at once, at a resolution sufficient for building atomic models. We have discovered structural and dynamic features that differentiate the ribosomes of P. falciparum from those of mammalian system. Prompted by the absence of RACK1 on the ribosome in our and an earlier study we confirmed that RACK1 does not specifically co-purify with the 80S fraction in schizonts. More extensive studies, using cryo-EM methodology, of translation in the parasite will provide structural knowledge that may lead to development of novel anti-malarials.

PubMed: 26432834
DOI: 10.1093/nar/gkv991

実験手法

ELECTRON MICROSCOPY (6.7 Å)