9E71

Cryo-EM structure of the Pyrobaculum calidifontis 70S ribosome

これはPDB形式変換不可エントリーです。

9E71 の概要

• エントリーDOI: 10.2210/pdb9e71/pdb
• 関連するPDBエントリー: 9E6Q
• EMDBエントリー: 47578 47628
• 分子名称: 5S rRNA, Large ribosomal subunit protein uL13, Large ribosomal subunit protein eL13, ... (72 entities in total)
• 機能のキーワード: ribosome, translation, hibernation, rna
• 由来する生物種: Pyrobaculum calidifontis JCM 11548; 詳細
• タンパク質・核酸の鎖数: 69
• 化学式量合計: 2559271.04

構造登録者

Nissley, A.J.,Cate, J.H.D. (登録日: 2024-10-31, 公開日: 2024-11-20, 最終更新日: 2025-08-13)

主引用文献

Nissley, A.J.,Shulgina, Y.,Kivimae, R.W.,Downing, B.E.,Penev, P.I.,Banfield, J.F.,Nayak, D.D.,Cate, J.H.D.
Structure of an archaeal ribosome reveals a divergent active site and hibernation factor.
Nat Microbiol, 10:1940-1953, 2025

PubMed Abstract: Ribosomes translate mRNA into protein. Despite divergence in ribosome structure over the course of evolution, the catalytic site, known as the peptidyl transferase centre (PTC), is thought to be nearly universally conserved. Here we identify clades of archaea that have highly divergent ribosomal RNA sequences in the PTC. To understand how these PTC sequences fold, we determined cryo-EM structures of the 70S and 50S ribosomes to 2.4 Å and 2 Å, respectively, from the hyperthermophilic archaeon Pyrobaculum calidifontis. PTC sequence variation leads to the rearrangement of key base triples, and differences between archaeal and bacterial ribosomal proteins enable sequence variation in archaeal PTCs. Finally, we identify an archaeal ribosome hibernation factor, Dri, that differs from known bacterial and eukaryotic hibernation factors and is found in multiple archaeal phyla. Overall, this work identifies factors that regulate ribosome function in archaea and reveals a larger diversity of the most ancient sequences in the ribosome.

PubMed: 40676158
DOI: 10.1038/s41564-025-02065-w

実験手法

ELECTRON MICROSCOPY (2.36 Å)