8A98

CRYO-EM STRUCTURE OF LEISHMANIA MAJOR 80S RIBOSOME : snoRNA MUTANT

これはPDB形式変換不可エントリーです。

8A98 の概要

• エントリーDOI: 10.2210/pdb8a98/pdb
• EMDBエントリー: 15272
• 分子名称: Putative 40S ribosomal protein S15, 40S ribosomal protein SA, Putative 40S ribosomal protein S3, ... (88 entities in total)
• 機能のキーワード: cryo-em, leishmania major, 80s ribosome snorna mutant, ribosome
• 由来する生物種: Leishmania major strain Friedlin; 詳細
• タンパク質・核酸の鎖数: 83
• 化学式量合計: 3486329.19

構造登録者

Rajan, K.S.,Yonath, A.,Bashan, A. (登録日: 2022-06-28, 公開日: 2023-10-11, 最終更新日: 2024-10-23)

主引用文献

Rajan, K.S.,Aryal, S.,Hiregange, D.G.,Bashan, A.,Madmoni, H.,Olami, M.,Doniger, T.,Cohen-Chalamish, S.,Pescher, P.,Taoka, M.,Nobe, Y.,Fedorenko, A.,Bose, T.,Zimermann, E.,Prina, E.,Aharon-Hefetz, N.,Pilpel, Y.,Isobe, T.,Unger, R.,Spath, G.F.,Yonath, A.,Michaeli, S.
Structural and mechanistic insights into the function of Leishmania ribosome lacking a single pseudouridine modification.
Cell Rep, 43:114203-114203, 2024

PubMed Abstract: Leishmania is the causative agent of cutaneous and visceral diseases affecting millions of individuals worldwide. Pseudouridine (Ψ), the most abundant modification on rRNA, changes during the parasite life cycle. Alterations in the level of a specific Ψ in helix 69 (H69) affected ribosome function. To decipher the molecular mechanism of this phenotype, we determine the structure of ribosomes lacking the single Ψ and its parental strain at ∼2.4-3 Å resolution using cryo-EM. Our findings demonstrate the significance of a single Ψ on H69 to its structure and the importance for its interactions with helix 44 and specific tRNAs. Our study suggests that rRNA modification affects translation of mRNAs carrying codon bias due to selective accommodation of tRNAs by the ribosome. Based on the high-resolution structures, we propose a mechanism explaining how the ribosome selects specific tRNAs.

PubMed: 38722744
DOI: 10.1016/j.celrep.2024.114203

実験手法

ELECTRON MICROSCOPY (2.46 Å)