4V9Q

Crystal Structure of Blasticidin S Bound to Thermus Thermophilus 70S Ribosome.

これはPDB形式変換不可エントリーです。

4V9Q の概要

• エントリーDOI: 10.2210/pdb4v9q/pdb
• 分子名称: 23S ribosomal RNA, 50S ribosomal protein L14, 50S ribosomal protein L15, ... (56 entities in total)
• 機能のキーワード: translation termination, peptidyl transfer, ribosomal crystal structure, translation inhibitor, blasticidin s, ribosome
• 由来する生物種: Thermus thermophilus; 詳細
• タンパク質・核酸の鎖数: 108
• 化学式量合計: 4417691.16

構造登録者

Svidritskiy, E.,Ling, C.,Ermolenko, D.N.,Korostelev, A.A. (登録日: 2013-06-12, 公開日: 2014-07-09, 最終更新日: 2026-01-14)

主引用文献

Svidritskiy, E.,Ling, C.,Ermolenko, D.N.,Korostelev, A.A.
Blasticidin S inhibits translation by trapping deformed tRNA on the ribosome.
Proc.Natl.Acad.Sci.USA, 110:12283-12288, 2013

PubMed Abstract: The antibiotic blasticidin S (BlaS) is a potent inhibitor of protein synthesis in bacteria and eukaryotes. We have determined a 3.4-Å crystal structure of BlaS bound to a 70S⋅tRNA ribosome complex and performed biochemical and single-molecule FRET experiments to determine the mechanism of action of the antibiotic. We find that BlaS enhances tRNA binding to the P site of the large ribosomal subunit and slows down spontaneous intersubunit rotation in pretranslocation ribosomes. However, the antibiotic has negligible effect on elongation factor G catalyzed translocation of tRNA and mRNA. The crystal structure of the antibiotic-ribosome complex reveals that BlaS impedes protein synthesis through a unique mechanism by bending the 3' terminus of the P-site tRNA toward the A site of the large ribosomal subunit. Biochemical experiments demonstrate that stabilization of the deformed conformation of the P-site tRNA by BlaS strongly inhibits peptidyl-tRNA hydrolysis by release factors and, to a lesser extent, peptide bond formation.

PubMed: 23824292
DOI: 10.1073/pnas.1304922110

実験手法

X-RAY DIFFRACTION (3.4 Å)