What recent ribosome structures have revealed about the mechanism of translation.
The high-resolution structures of ribosomal subunits published in 2000 have revolutionized the field of protein translation. They facilitated the determination and interpretation of functional complexes of the ribosome by crystallography and electron microscopy. Knowledge of the precise positions of residues in the ribosome in various states has facilitated increasingly sophisticated biochemical and genetic experiments, as well as the use of new methods such as single-molecule kinetics. In this review, we discuss how the interaction between structural and functional studies over the last decade has led to a deeper understanding of the complex mechanisms underlying translation.
MRC Laboratory of Molecular Biology, Cambridge CB2 0QH, UK. schmeing@mrc-lmb.cam.ac.uk
T Martin
TM
Schmeing
V
V
Ramakrishnan
D001426:Bacterial Proteins / Q000737:chemistry / Q000378:metabolism; D055162:Biocatalysis; D014176:Protein Biosynthesis / Q000502:physiology*; D012269:Ribosomal Proteins / Q000378:metabolism; D012270:Ribosomes / Q000737:chemistry* / Q000378:metabolism*; D013329:Structure-Activity Relationship
D001426:Bacterial Proteins; D012269:Ribosomal Proteins