6B4V
Antibiotic blasticidin S and E. coli release factor 1 bound to the 70S ribosome
This is a non-PDB format compatible entry.
Summary for 6B4V
Entry DOI | 10.2210/pdb6b4v/pdb |
Descriptor | 16S ribosomal RNA, 50S ribosomal protein L9, 50S ribosomal protein L13, ... (58 entities in total) |
Functional Keywords | termination suppression, class i release factors, rf1, stop-codon recognition, termination, blasticidin s, ribosome-antibiotic complex, ribosome/antibiotic |
Biological source | Thermus thermophilus HB27 More |
Total number of polymer chains | 112 |
Total formula weight | 4544266.41 |
Authors | Svidritskiy, E.,Korostelev, A.A. (deposition date: 2017-09-27, release date: 2018-02-07, Last modification date: 2025-03-19) |
Primary citation | Svidritskiy, E.,Korostelev, A.A. Mechanism of Inhibition of Translation Termination by Blasticidin S. J. Mol. Biol., 430:591-593, 2018 Cited by PubMed Abstract: Understanding the mechanisms of inhibitors of translation termination may inform development of new antibacterials and therapeutics for premature termination diseases. We report the crystal structure of the potent termination inhibitor blasticidin S bound to the ribosomal 70S•release factor 1 (RF1) termination complex. Blasticidin S shifts the catalytic domain 3 of RF1 and restructures the peptidyl transferase center. Universally conserved uridine 2585 in the peptidyl transferase center occludes the catalytic backbone of the GGQ motif of RF1, explaining the structural mechanism of inhibition. Rearrangement of domain 3 relative to the codon-recognition domain 2 provides insight into the dynamics of RF1 implicated in termination accuracy. PubMed: 29366636DOI: 10.1016/j.jmb.2018.01.007 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (3.4 Å) |
Structure validation
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