A decade of progress in understanding the structural basis of protein synthesis
(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)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/948936
- author
- Al-Karadaghi, Salam LU ; Kristensen, O and Liljas, Anders LU
- organization
- publishing date
- 2000
- 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
- 2016-04-01 11:47:27
- date last changed
- 2022-01-26 18:18:57
@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}},
doi = {{10.1016/S0079-6107(00)00005-5}},
volume = {{73}},
year = {{2000}},
}