2OTJ

13-deoxytedanolide bound to the large subunit of Haloarcula marismortui

2OTJ の概要

• エントリーDOI: 10.2210/pdb2otj/pdb
• 関連するPDBエントリー: 1S72 2OTL
• 分子名称: 23S ribosomal RNA, 50S ribosomal protein L10e, 50S ribosomal protein L13P, ... (38 entities in total)
• 機能のキーワード: 13 deoxytedanolide, antibiotic complex, 50s, ribosome
• 由来する生物種: Haloarcula marismortui; 詳細
• 細胞内の位置: Cytoplasm : P12743
• タンパク質・核酸の鎖数: 31
• 化学式量合計: 1478889.74

構造登録者

Blaha, G.,Schroeder, S.J.,Tirado-Rives, J. (登録日: 2007-02-08, 公開日: 2007-04-03, 最終更新日: 2023-08-30)

主引用文献

Schroeder, S.J.,Blaha, G.,Tirado-Rives, J.,Steitz, T.A.,Moore, P.B.
The Structures of Antibiotics Bound to the E Site Region of the 50 S Ribosomal Subunit of Haloarcula marismortui: 13-Deoxytedanolide and Girodazole.
J.Mol.Biol., 367:1471-1479, 2007

PubMed Abstract: Crystal structures of the 50 S ribosomal subunit from Haloarcula marismortui complexed with two antibiotics have identified new sites at which antibiotics interact with the ribosome and inhibit protein synthesis. 13-Deoxytedanolide binds to the E site of the 50 S subunit at the same location as the CCA of tRNA, and thus appears to inhibit protein synthesis by competing with deacylated tRNAs for E site binding. Girodazole binds near the E site region, but is somewhat buried and may inhibit tRNA binding by interfering with conformational changes that occur at the E site. The specificity of 13-deoxytedanolide for eukaryotic ribosomes is explained by its extensive interactions with protein L44e, which is an E site component of archaeal and eukaryotic ribosomes, but not of eubacterial ribosomes. In addition, protein L28, which is unique to the eubacterial E site, overlaps the site occupied by 13-deoxytedanolide, precluding its binding to eubacterial ribosomes. Girodazole is specific for eukarytes and archaea because it makes interactions with L15 that are not possible in eubacteria.

PubMed: 17321546
DOI: 10.1016/j.jmb.2007.01.081

実験手法

X-RAY DIFFRACTION (2.9 Å)