3CF5
Thiopeptide antibiotic Thiostrepton bound to the large ribosomal subunit of Deinococcus radiodurans
3CF5 の概要
エントリーDOI | 10.2210/pdb3cf5/pdb |
関連するPDBエントリー | 1D8T 1E9W 1OLN 2C77 2JQ7 2ZJP |
関連するBIRD辞書のPRD_ID | PRD_000223 |
分子名称 | 50S RIBOSOMAL PROTEIN L33, 50S RIBOSOMAL PROTEIN L6, 50S RIBOSOMAL PROTEIN L11, ... (32 entities in total) |
機能のキーワード | ribosome-antibiotic complex, antibiotic, ribosome, thiostrepton, rna, l11, thiopeptide, thiazole, thiazoline, pyridine, translation inhibition, ribosome/antibiotic |
由来する生物種 | DEINOCOCCUS RADIODURANS 詳細 |
タンパク質・核酸の鎖数 | 31 |
化学式量合計 | 1367119.57 |
構造登録者 | Harms, J.M.,Wilson, D.N.,Schluenzen, F.,Connell, S.R.,Stachelhaus, T.,Zaborowska, Z.,Spahn, C.M.T.,Fucini, P. (登録日: 2008-03-02, 公開日: 2008-06-17, 最終更新日: 2023-11-15) |
主引用文献 | Harms, J.M.,Wilson, D.N.,Schluenzen, F.,Connell, S.R.,Stachelhaus, T.,Zaborowska, Z.,Spahn, C.M.,Fucini, P. Translational Regulation Via L11: Molecular Switches on the Ribosome Turned on and Off by Thiostrepton and Micrococcin. Mol.Cell, 30:26-, 2008 Cited by PubMed Abstract: The thiopeptide class of antibiotics targets the GTPase-associated center (GAC) of the ribosome to inhibit translation factor function. Using X-ray crystallography, we have determined the binding sites of thiostrepton (Thio), nosiheptide (Nosi), and micrococcin (Micro), on the Deinococcus radiodurans large ribosomal subunit. The thiopeptides, by binding within a cleft located between the ribosomal protein L11 and helices 43 and 44 of the 23S rRNA, overlap with the position of domain V of EF-G, thus explaining how this class of drugs perturbs translation factor binding to the ribosome. The presence of Micro leads to additional density for the C-terminal domain (CTD) of L7, adjacent to and interacting with L11. The results suggest that L11 acts as a molecular switch to control L7 binding and plays a pivotal role in positioning one L7-CTD monomer on the G' subdomain of EF-G to regulate EF-G turnover during protein synthesis. PubMed: 18406324DOI: 10.1016/J.MOLCEL.2008.01.009 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (3.3 Å) |
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