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Title: Structures of the Ribosome in Intermediate States of Ratcheting

Abstract

Protein biosynthesis on the ribosome requires repeated cycles of ratcheting, which couples rotation of the two ribosomal subunits with respect to each other, and swiveling of the head domain of the small subunit. However, the molecular basis for how the two ribosomal subunits rearrange contacts with each other during ratcheting while remaining stably associated is not known. Here, we describe x-ray crystal structures of the intact Escherichia coli ribosome, either in the apo-form (3.5 angstrom resolution) or with one (4.0 angstrom resolution) or two (4.0 angstrom resolution) anticodon stem-loop tRNA mimics bound, that reveal intermediate states of intersubunit rotation. In the structures, the interface between the small and large ribosomal subunits rearranges in discrete steps along the ratcheting pathway. Positioning of the head domain of the small subunit is controlled by interactions with the large subunit and with the tRNA bound in the peptidyl-tRNA site. The intermediates observed here provide insight into how tRNAs move into the hybrid state of binding that precedes the final steps of mRNA and tRNA translocation.

Authors:
; ; ;  [1];  [1]
  1. (
Publication Date:
Research Org.:
Argonne National Lab. (ANL), Argonne, IL (United States)
Sponsoring Org.:
USDOE
OSTI Identifier:
1005865
Resource Type:
Journal Article
Journal Name:
Science
Additional Journal Information:
Journal Volume: 325; Journal Issue: 08, 2009; Journal ID: ISSN 0193-4511
Country of Publication:
United States
Language:
ENGLISH
Subject:
36 MATERIALS SCIENCE; BIOSYNTHESIS; CRYSTAL STRUCTURE; ESCHERICHIA COLI; POSITIONING; PROTEINS; RATCHETING; RESOLUTION; RIBOSOMES; ROTATION; TRANSLOCATION

Citation Formats

Zhang, Wen, Dunkle, Jack A., Cate, Jamie H.D., UCB), and LBNL). Structures of the Ribosome in Intermediate States of Ratcheting. United States: N. p., 2009. Web. doi:10.1126/science.1175275.
Zhang, Wen, Dunkle, Jack A., Cate, Jamie H.D., UCB), & LBNL). Structures of the Ribosome in Intermediate States of Ratcheting. United States. doi:10.1126/science.1175275.
Zhang, Wen, Dunkle, Jack A., Cate, Jamie H.D., UCB), and LBNL). Wed . "Structures of the Ribosome in Intermediate States of Ratcheting". United States. doi:10.1126/science.1175275.
@article{osti_1005865,
title = {Structures of the Ribosome in Intermediate States of Ratcheting},
author = {Zhang, Wen and Dunkle, Jack A. and Cate, Jamie H.D. and UCB) and LBNL)},
abstractNote = {Protein biosynthesis on the ribosome requires repeated cycles of ratcheting, which couples rotation of the two ribosomal subunits with respect to each other, and swiveling of the head domain of the small subunit. However, the molecular basis for how the two ribosomal subunits rearrange contacts with each other during ratcheting while remaining stably associated is not known. Here, we describe x-ray crystal structures of the intact Escherichia coli ribosome, either in the apo-form (3.5 angstrom resolution) or with one (4.0 angstrom resolution) or two (4.0 angstrom resolution) anticodon stem-loop tRNA mimics bound, that reveal intermediate states of intersubunit rotation. In the structures, the interface between the small and large ribosomal subunits rearranges in discrete steps along the ratcheting pathway. Positioning of the head domain of the small subunit is controlled by interactions with the large subunit and with the tRNA bound in the peptidyl-tRNA site. The intermediates observed here provide insight into how tRNAs move into the hybrid state of binding that precedes the final steps of mRNA and tRNA translocation.},
doi = {10.1126/science.1175275},
journal = {Science},
issn = {0193-4511},
number = 08, 2009,
volume = 325,
place = {United States},
year = {2009},
month = {10}
}