5OPT

Structure of KSRP in context of Trypanosoma cruzi 40S

5OPT の概要

• エントリーDOI: 10.2210/pdb5opt/pdb
• EMDBエントリー: 3844
• 分子名称: Activated protein kinase C receptor, putative, 40S ribosomal protein S13, putative, 40S ribosomal protein S27, putative, ... (35 entities in total)
• 機能のキーワード: kinetoplastids, ribosome, cryo-em, ksrp
• 由来する生物種: Trypanosoma cruzi (strain CL Brener); 詳細
• 細胞内の位置: Cytoplasm : Q4DZ41 Q4CQ63
• タンパク質・核酸の鎖数: 35
• 化学式量合計: 1416991.87

構造登録者

Brito Querido, J.,Mancera-Martinez, E.,Vicens, Q.,Bochler, A.,Chicher, J.,Simonetti, A.,Hashem, Y. (登録日: 2017-08-10, 公開日: 2017-11-15, 最終更新日: 2024-11-20)

主引用文献

Brito Querido, J.,Mancera-Martinez, E.,Vicens, Q.,Bochler, A.,Chicher, J.,Simonetti, A.,Hashem, Y.
The cryo-EM Structure of a Novel 40S Kinetoplastid-Specific Ribosomal Protein.
Structure, 25:1785-1794.e3, 2017

PubMed Abstract: Kinetoplastids are potentially lethal protozoan pathogens affecting more than 20 million people worldwide. There is a critical need for more specific targets for the development of safer anti-kinetoplastid therapeutic molecules that can replace the scarce and highly cytotoxic current drugs. The kinetoplastid ribosome represents a potential therapeutic target due to its relative structural divergence when compared with its human counterpart. However, several kinetoplastid-specific ribosomal features remain uncharacterized. Here, we present the near-atomic cryoelectron microscopy structure of a novel bona fide kinetoplastid-specific ribosomal (r-) protein (KSRP) bound to the ribosome. KSRP is an essential protein located at the solvent face of the 40S subunit, where it binds and stabilizes kinetoplastid-specific domains of rRNA, suggesting its role in ribosome integrity. KSRP also interacts with the r-protein eS6 at a region that is only conserved in kinetoplastids. The kinetoplastid-specific ribosomal environment of KSRP provides a promising target for the design of safer anti-kinetoplastidian drugs.

PubMed: 29107485
DOI: 10.1016/j.str.2017.09.014

実験手法

ELECTRON MICROSCOPY (4 Å)