Nature Structural Biology
7, 855 - 861 (2000)
doi:10.1038/79603
Approaching translation at atomic resolutionJoseph D. Puglisi1, Scott C. Blanchard1
& Rachel Green21
Department of Structural Biology, Stanford University School of Medicine, Stanford, California 21205, 94305-5126, USA. 2
Howard Hughes Medical Institute and Department of Molecular Biology and Genetics, The Johns Hopkins University School of Medicine, Baltimore, Maryland 21205, USA.
Correspondence should be addressed to Joseph D. Puglisi puglisi@stanford.edu or Rachel Green ragreen@jhmi.eduAtomic resolution structures of 50S and 30S ribosomal particles have recently been solved by X-ray diffraction. These ribosomal structures show often unusual folds of ribosomal RNAs and proteins, and provide molecular explanations for fundamental aspects of translation. In the 50S structure, the active site for peptide bond formation was localized and found to consist of RNA. The ribosome is thus a ribozyme. In the 30S structures, tRNA binding sites were located, and molecular mechanisms for ribosomal fidelity were proposed. The 30S subunit particle has three globular domains, and relative movements of these domains may be required for translocation of the ribosome during protein synthesis. The structures are consistent with and rationalize decades of biochemical analysis of translation and usher in a molecular age in understanding the ribosome.
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