Structure and structural variations of the Escherichia coli 30 S ribosomal subunit as revealed by three-dimensional cryo-electron microscopy 1 1 Edited by W. Baumeister

Structure and structural variations of the Escherichia coli 30 S ribosomal subunit as revealed by... A three-dimensional reconstruction of the 30 S subunit of the Escherichia coli ribosome was obtained at 23 Å resolution. Because of the improved resolution, many more structural details are seen as compared to those obtained in earlier studies. Thus, the new structure is more suitable for comparison with the 30 S subunit part of the 70 S ribosome, whose structure is already known at a better resolution. In addition, we observe relative and, to some extent, independent movements of three main structural domains of the 30 S subunit, namely head, platform and the main body, which lead to partial blurring of the reconstructed volume. An attempt to subdivide the data set into conformationally defined subsets reveals the existence of conformers in which these domains have different orientations with respect to one another. This result suggests the existence of dynamic properties of the 30 S subunit that might be required for facilitating its interactions with mRNA, tRNA and other ligands during protein biosynthesis. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Journal of Molecular Biology Elsevier

Structure and structural variations of the Escherichia coli 30 S ribosomal subunit as revealed by three-dimensional cryo-electron microscopy 1 1 Edited by W. Baumeister

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Publisher
Elsevier
Copyright
Copyright © 1999 Academic Press
ISSN
0022-2836
DOI
10.1006/jmbi.1999.2538
pmid
10064696
Publisher site
See Article on Publisher Site

Abstract

A three-dimensional reconstruction of the 30 S subunit of the Escherichia coli ribosome was obtained at 23 Å resolution. Because of the improved resolution, many more structural details are seen as compared to those obtained in earlier studies. Thus, the new structure is more suitable for comparison with the 30 S subunit part of the 70 S ribosome, whose structure is already known at a better resolution. In addition, we observe relative and, to some extent, independent movements of three main structural domains of the 30 S subunit, namely head, platform and the main body, which lead to partial blurring of the reconstructed volume. An attempt to subdivide the data set into conformationally defined subsets reveals the existence of conformers in which these domains have different orientations with respect to one another. This result suggests the existence of dynamic properties of the 30 S subunit that might be required for facilitating its interactions with mRNA, tRNA and other ligands during protein biosynthesis.

Journal

Journal of Molecular BiologyElsevier

Published: Mar 12, 1999

References

  • Conformational variability in Escherichia coli 70S ribosome as revealed by 3D cryo-electron microscopy
    Agrawal, R.K.; Lata, R.K.; Frank, J.
  • Effects of Mg 2+ , K + and H + on an equilibrium between alternative conformations of an RNA pseudoknot
    Gluick, T.C.; Gerstner, R.B.; Draper, D.E.
  • Evidence for in vivo ribosome recycling, the fourth step in protein biosynthesis
    Janosi, L.; Mottagui-Tabar, S.; Isaksson, L.A.; Sekine, Y.; Ohtsubo, E.; Zhang, S.; Goon, S.; Nelken, S.; Shuda, M.; Kaji, A.
  • Three-dimensional reconstruction of the Escherichia coli 30 S ribosomal subunit in ice
    Lata, K.R.; Agrawal, R.K.; Penczek, P.; Grassucci, R.; Zhu, J.; Frank, J.
  • Late events in translation initiation-adjustment of fMet-tRNA in the ribosomal P-site
    La Teana, A.; Pon, C.L.; Gualerzi, C.O.
  • Structural dynamics of translating ribosomes
    Laughrea, M.
  • A new model for the three-dimensional folding of Escherichia coli 16 S ribosomal RNA. II. The RNA-protein interaction data
    Müller, F.; Brimacombe, R.
  • Protein and Mg 2+ -induced conformational changes in the S15 binding site of 16 S ribosomal RNA
    Orr, J.W.; Hagerman, P.J.; Williamson, J.R.
  • Three-dimensional reconstruction with contrast transfer function correction from energy-filtered cryoelectron micrographs
    Zhu, J.; Penczek, P.A.; Schröder, R.; Frank, J.

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