2JQ7

Model for thiostrepton binding to the ribosomal L11-RNA

「2NYO」から置き換えられました

2JQ7 の概要

• エントリーDOI: 10.2210/pdb2jq7/pdb
• 関連するPDBエントリー: 1D8T 1E9W 1MMS 1OLN 2C77 2ZJP 3CF5
• 関連するBIRD辞書のPRD_ID: PRD_000223
• 分子名称: 50S RIBOSOMAL PROTEIN L11, RIBOSOMAL RNA, THIOSTREPTON (3 entities in total)
• 機能のキーワード: ribosome-antibiotic complex, thiopeptide, antibacterial, thiazole, thiazoline, oxazole, ribosome, l11, translation inhibition, ribosome/antibiotic
• 由来する生物種: THERMOTOGA MARITIMA; 詳細
• 細胞内の位置: Secreted : P0C8P8
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 35611.05

構造登録者

Jonker, H.R.A.,Ilin, S.,Grimm, S.K.,Woehnert, J.,Schwalbe, H. (登録日: 2007-05-30, 公開日: 2007-07-03, 最終更新日: 2021-08-18)

主引用文献

Jonker, H.R.A.,Ilin, S.,Grimm, S.K.,Woehnert, J.,Schwalbe, H.
L11 Domain Rearrangement Upon Binding to RNA and Thiostrepton Studied by NMR Spectroscopy
Nucleic Acids Res., 35:441-, 2007

PubMed Abstract: Ribosomal proteins are assumed to stabilize specific RNA structures and promote compact folding of the large rRNA. The conformational dynamics of the protein between the bound and unbound state play an important role in the binding process. We have studied those dynamical changes in detail for the highly conserved complex between the ribosomal protein L11 and the GTPase region of 23S rRNA. The RNA domain is compactly folded into a well defined tertiary structure, which is further stabilized by the association with the C-terminal domain of the L11 protein (L11(ctd)). In addition, the N-terminal domain of L11 (L11(ntd)) is implicated in the binding of the natural thiazole antibiotic thiostrepton, which disrupts the elongation factor function. We have studied the conformation of the ribosomal protein and its dynamics by NMR in the unbound state, the RNA bound state and in the ternary complex with the RNA and thiostrepton. Our data reveal a rearrangement of the L11(ntd), placing it closer to the RNA after binding of thiostrepton, which may prevent binding of elongation factors. We propose a model for the ternary L11-RNA-thiostrepton complex that is additionally based on interaction data and conformational information of the L11 protein. The model is consistent with earlier findings and provides an explanation for the role of L11(ntd) in elongation factor binding.

PubMed: 17169991
DOI: 10.1093/NAR/GKL1066

実験手法

SOLUTION NMR