4V9Q
Crystal Structure of Blasticidin S Bound to Thermus Thermophilus 70S Ribosome.
This is a non-PDB format compatible entry.
Summary for 4V9Q
| Entry DOI | 10.2210/pdb4v9q/pdb |
| Descriptor | 23S ribosomal RNA, 50S ribosomal protein L14, 50S ribosomal protein L15, ... (56 entities in total) |
| Functional Keywords | translation termination, peptidyl transfer, ribosomal crystal structure, translation inhibitor, blasticidin s, ribosome |
| Biological source | Thermus thermophilus More |
| Total number of polymer chains | 108 |
| Total formula weight | 4417691.16 |
| Authors | Svidritskiy, E.,Ling, C.,Ermolenko, D.N.,Korostelev, A.A. (deposition date: 2013-06-12, release date: 2014-07-09, Last modification date: 2024-10-30) |
| Primary citation | 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 Cited by 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: 23824292DOI: 10.1073/pnas.1304922110 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.4 Å) |
Structure validation
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