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Title: Blasticidin S inhibits translation by trapping deformed tRNA on the ribosome

Authors:
; ; ;  [1];  [2]
  1. (Rochester-Med)
  2. (
Publication Date:
Research Org.:
Argonne National Lab. (ANL), Argonne, IL (United States). Advanced Photon Source (APS)
Sponsoring Org.:
UNIVERSITYNIH
OSTI Identifier:
1092608
Resource Type:
Journal Article
Resource Relation:
Journal Name: Proc. Natl. Acad. Sci. USA; Journal Volume: 110; Journal Issue: (30) ; 07, 2013
Country of Publication:
United States
Language:
ENGLISH

Citation Formats

Svidritskiy, Egor, Ling, Clarence, Ermolenko, Dmitri N., Korostelev, Andrei A., and UMASS, MED). Blasticidin S inhibits translation by trapping deformed tRNA on the ribosome. United States: N. p., 2013. Web. doi:10.1073/pnas.1304922110.
Svidritskiy, Egor, Ling, Clarence, Ermolenko, Dmitri N., Korostelev, Andrei A., & UMASS, MED). Blasticidin S inhibits translation by trapping deformed tRNA on the ribosome. United States. doi:10.1073/pnas.1304922110.
Svidritskiy, Egor, Ling, Clarence, Ermolenko, Dmitri N., Korostelev, Andrei A., and UMASS, MED). Mon . "Blasticidin S inhibits translation by trapping deformed tRNA on the ribosome". United States. doi:10.1073/pnas.1304922110.
@article{osti_1092608,
title = {Blasticidin S inhibits translation by trapping deformed tRNA on the ribosome},
author = {Svidritskiy, Egor and Ling, Clarence and Ermolenko, Dmitri N. and Korostelev, Andrei A. and UMASS, MED)},
abstractNote = {},
doi = {10.1073/pnas.1304922110},
journal = {Proc. Natl. Acad. Sci. USA},
number = (30) ; 07, 2013,
volume = 110,
place = {United States},
year = {Mon Sep 23 00:00:00 EDT 2013},
month = {Mon Sep 23 00:00:00 EDT 2013}
}
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  • During protein synthesis, the ribosome controls the movement of tRNA and mRNA by means of large-scale structural rearrangements. We describe structures of the intact bacterial ribosome from Escherichia coli that reveal how the ribosome binds tRNA in two functionally distinct states, determined to a resolution of {approx}3.2 angstroms by means of x-ray crystallography. One state positions tRNA in the peptidyl-tRNA binding site. The second, a fully rotated state, is stabilized by ribosome recycling factor and binds tRNA in a highly bent conformation in a hybrid peptidyl/exit site. The structures help to explain how the ratchet-like motion of the two ribosomalmore » subunits contributes to the mechanisms of translocation, termination, and ribosome recycling.« less