7KWG
Staphylococcus aureus 30S ribosomal subunit in presence of spermidine
7KWG の概要
| エントリーDOI | 10.2210/pdb7kwg/pdb |
| EMDBエントリー | 23052 |
| 分子名称 | mRNA, 30S ribosomal protein S9, 30S ribosomal protein S10, ... (21 entities in total) |
| 機能のキーワード | pathogen, small ribosomal subunit, spermidine, ribosome |
| 由来する生物種 | Staphylococcus aureus subsp. aureus NCTC 8325 詳細 |
| タンパク質・核酸の鎖数 | 21 |
| 化学式量合計 | 788854.46 |
| 構造登録者 | Belinite, M.,Khusainov, I.,Marzi, S.,Romby, P.,Yusupov, M.,Hashem, Y. (登録日: 2020-11-30, 公開日: 2021-01-27, 最終更新日: 2024-05-29) |
| 主引用文献 | Belinite, M.,Khusainov, I.,Soufari, H.,Marzi, S.,Romby, P.,Yusupov, M.,Hashem, Y. Stabilization of Ribosomal RNA of the Small Subunit by Spermidine in Staphylococcus aureus . Front Mol Biosci, 8:738752-738752, 2021 Cited by PubMed Abstract: Cryo-electron microscopy is now used as a method of choice in structural biology for studying protein synthesis, a process mediated by the ribosome machinery. In order to achieve high-resolution structures using this approach, one needs to obtain homogeneous and stable samples, which requires optimization of ribosome purification in a species-dependent manner. This is especially critical for the bacterial small ribosomal subunit that tends to be unstable in the absence of ligands. Here, we report a protocol for purification of stable 30 S from the Gram-positive bacterium and its cryo-EM structures: in presence of spermidine at a resolution ranging between 3.4 and 3.6 Å and in its absence at 5.3 Å. Using biochemical characterization and cryo-EM, we demonstrate the importance of spermidine for stabilization of the 30 S preserving favorable conformation of the helix 44. PubMed: 34869582DOI: 10.3389/fmolb.2021.738752 主引用文献が同じPDBエントリー |
| 実験手法 | ELECTRON MICROSCOPY (3.75 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






