Ribosome structure and the mechanism of translation.
The publication of crystal structures of the 50S and 30S ribosomal subunits and the intact 70S ribosome is revolutionizing our understanding of protein synthesis. This review is an attempt to correlate the structures with biochemical and genetic data to identify the gaps and limits in our current knowledge of the mechanisms involved in translation.
Ramakrishnan
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MRC Laboratory of Molecular Biology, Hills Road, Cambridge CB2 2QH, United Kingdom. ramak@mrc-lmb.cam.ac.uk
D001419:Bacteria / Q000235:genetics; D001426:Bacterial Proteins / Q000378:metabolism; D008957:Models, Genetic; D008958:Models, Molecular; D010441:Peptide Chain Elongation, Translational; D010444:Peptide Elongation Factor Tu / Q000378:metabolism; D010448:Peptide Initiation Factors / Q000378:metabolism; D010454:Peptide Termination Factors / Q000378:metabolism; D010458:Peptidyl Transferases / Q000378:metabolism; D014176:Protein Biosynthesis; D020836:Protein Structure, Quaternary; D021122:Protein Subunits; D012333:RNA, Messenger / Q000378:metabolism; D012270:Ribosomes / Q000737:chemistry / Q000378:metabolism*
D001426:Bacterial Proteins; D010448:Peptide Initiation Factors; D010454:Peptide Termination Factors; D021122:Protein Subunits; D012333:RNA, Messenger; D010458:Peptidyl Transferases; D010444:Peptide Elongation Factor Tu