8EIU の概要
| エントリーDOI | 10.2210/pdb8eiu/pdb |
| EMDBエントリー | 28165 28218 28229 28230 |
| 分子名称 | 50S ribosomal protein L33, 30S ribosomal protein S5, 30S ribosomal protein S6, ... (62 entities in total) |
| 機能のキーワード | rna, thermophile, a loop, ribosome |
| 由来する生物種 | Escherichia coli 詳細 |
| タンパク質・核酸の鎖数 | 55 |
| 化学式量合計 | 2208400.96 |
| 構造登録者 | Nissley, A.J.,Penev, P.I.,Watson, Z.L.,Banfield, J.F.,Cate, J.H.D. (登録日: 2022-09-15, 公開日: 2023-02-01, 最終更新日: 2025-03-19) |
| 主引用文献 | Nissley, A.J.,Penev, P.I.,Watson, Z.L.,Banfield, J.F.,Cate, J.H.D. Rare ribosomal RNA sequences from archaea stabilize the bacterial ribosome. Nucleic Acids Res., 51:1880-1894, 2023 Cited by PubMed Abstract: The ribosome serves as the universally conserved translator of the genetic code into proteins and supports life across diverse temperatures ranging from below freezing to above 120°C. Ribosomes are capable of functioning across this wide range of temperatures even though the catalytic site for peptide bond formation, the peptidyl transferase center, is nearly universally conserved. Here we find that Thermoproteota, a phylum of thermophilic Archaea, substitute cytidine for uridine at large subunit rRNA positions 2554 and 2555 (Escherichia coli numbering) in the A loop, immediately adjacent to the binding site for the 3'-end of A-site tRNA. We show by cryo-EM that E. coli ribosomes with uridine to cytidine mutations at these positions retain the proper fold and post-transcriptional modification of the A loop. Additionally, these mutations do not affect cellular growth, protect the large ribosomal subunit from thermal denaturation, and increase the mutational robustness of nucleotides in the peptidyl transferase center. This work identifies sequence variation across archaeal ribosomes in the peptidyl transferase center that likely confers stabilization of the ribosome at high temperatures and develops a stable mutant bacterial ribosome that can act as a scaffold for future ribosome engineering efforts. PubMed: 36660825DOI: 10.1093/nar/gkac1273 主引用文献が同じPDBエントリー |
| 実験手法 | ELECTRON MICROSCOPY (2.24 Å) |
構造検証レポート
検証レポート(詳細版)
をダウンロード






