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Mechanism of Inhibition of Translation Termination by Blasticidin S

Journal of molecular biology | 26 Jan 2018

E Svidritskiy and AA Korostelev
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 BlaS bound to the ribosomal 70S•RF1 termination complex. BlaS 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.
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Concepts
Solid, Bacteria, Xanthine oxidase inhibitor, Ribosome, Inhibitor, Peptidyl transferase, Enzyme inhibitor, Enzyme
MeSH headings
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