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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 DOI10.2210/pdb6b4v/pdb
Descriptor16S ribosomal RNA, 50S ribosomal protein L9, 50S ribosomal protein L13, ... (58 entities in total)
Functional Keywordstermination suppression, class i release factors, rf1, stop-codon recognition, termination, blasticidin s, ribosome-antibiotic complex, ribosome/antibiotic
Biological sourceThermus thermophilus HB27
More
Total number of polymer chains112
Total formula weight4544266.41
Authors
Svidritskiy, E.,Korostelev, A.A. (deposition date: 2017-09-27, release date: 2018-02-07, Last modification date: 2025-03-19)
Primary citationSvidritskiy, 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: 29366636
DOI: 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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