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A decade of progress in understanding the structural basis of protein synthesis

Al-Karadaghi, Salam LU ; Kristensen, O and Liljas, Anders LU (2000) In Progress in Biophysics and Molecular Biology 73(2). p.167-193
Abstract
The key reaction of protein synthesis, peptidyl transfer, is catalysed in all living organisms by the ribosome - an advanced and highly efficient molecular machine. During the last decade extensive X-ray crystallographic and NMR studies of the three-dimensional structure of ribosomal proteins, ribosomal RNA components and their complexes with ribosomal proteins, and of several translation factors in different functional states have taken us to a new level of understanding of the mechanism of function of the protein synthesis machinery. Among the new remarkable features revealed by structural studies, is the mimicry of the tRNA molecule by elongation factor G, ribosomal recycling factor and the eukaryotic release factor 1. Several other... (More)
The key reaction of protein synthesis, peptidyl transfer, is catalysed in all living organisms by the ribosome - an advanced and highly efficient molecular machine. During the last decade extensive X-ray crystallographic and NMR studies of the three-dimensional structure of ribosomal proteins, ribosomal RNA components and their complexes with ribosomal proteins, and of several translation factors in different functional states have taken us to a new level of understanding of the mechanism of function of the protein synthesis machinery. Among the new remarkable features revealed by structural studies, is the mimicry of the tRNA molecule by elongation factor G, ribosomal recycling factor and the eukaryotic release factor 1. Several other translation factors, for which three-dimensional structures are not yet known, are also expected to show some form of tRNA mimicry. The efforts of several crystallographic and biochemical groups have resulted in the determination by X-ray crystallography of the structures of the 30S and 50S subunits at moderate resolution, and of the structure of the 70S subunit both by X-ray crystallography and cryo-electron microscopy (EM). In addition, low resolution cryo-EM models of the ribosome with different translation factors and tRNA have been obtained. The new ribosomal models allowed for the first time a clear identification of the functional centres of the ribosome and of the binding sites for tRNA and ribosomal proteins with known three-dimensional structure. The new structural data have opened a way for the design of new experiments aimed at deeper understanding at an atomic level of the dynamics of the system. (Less)
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organization
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type
Contribution to journal
publication status
published
subject
in
Progress in Biophysics and Molecular Biology
volume
73
issue
2
pages
167 - 193
publisher
Elsevier
external identifiers
  • scopus:0033823156
ISSN
1873-1732
DOI
10.1016/S0079-6107(00)00005-5
language
English
LU publication?
yes
id
2fb7155f-2360-4bd5-95fa-e3390d1f5993 (old id 948936)
date added to LUP
2008-01-24 14:13:39
date last changed
2017-01-01 04:32:44
@article{2fb7155f-2360-4bd5-95fa-e3390d1f5993,
  abstract     = {The key reaction of protein synthesis, peptidyl transfer, is catalysed in all living organisms by the ribosome - an advanced and highly efficient molecular machine. During the last decade extensive X-ray crystallographic and NMR studies of the three-dimensional structure of ribosomal proteins, ribosomal RNA components and their complexes with ribosomal proteins, and of several translation factors in different functional states have taken us to a new level of understanding of the mechanism of function of the protein synthesis machinery. Among the new remarkable features revealed by structural studies, is the mimicry of the tRNA molecule by elongation factor G, ribosomal recycling factor and the eukaryotic release factor 1. Several other translation factors, for which three-dimensional structures are not yet known, are also expected to show some form of tRNA mimicry. The efforts of several crystallographic and biochemical groups have resulted in the determination by X-ray crystallography of the structures of the 30S and 50S subunits at moderate resolution, and of the structure of the 70S subunit both by X-ray crystallography and cryo-electron microscopy (EM). In addition, low resolution cryo-EM models of the ribosome with different translation factors and tRNA have been obtained. The new ribosomal models allowed for the first time a clear identification of the functional centres of the ribosome and of the binding sites for tRNA and ribosomal proteins with known three-dimensional structure. The new structural data have opened a way for the design of new experiments aimed at deeper understanding at an atomic level of the dynamics of the system.},
  author       = {Al-Karadaghi, Salam and Kristensen, O and Liljas, Anders},
  issn         = {1873-1732},
  language     = {eng},
  number       = {2},
  pages        = {167--193},
  publisher    = {Elsevier},
  series       = {Progress in Biophysics and Molecular Biology},
  title        = {A decade of progress in understanding the structural basis of protein synthesis},
  url          = {http://dx.doi.org/10.1016/S0079-6107(00)00005-5},
  volume       = {73},
  year         = {2000},
}