The ribosome-structure and functional ligand-binding experiments using cryo-electron microscopy.
Cryo-electron microscopy has greatly advanced our understanding of the basic steps of protein synthesis in the bacterial ribosome. This article gives an overview of what has been achieved so far. Through three-dimensional visualization of complexes that represent the ribosome in defined binding states, locations were derived for the tRNA in A, P, and E sites, as well as the elongation factors. In addition, the pathways of messenger RNA and the exiting polypeptide chain could be inferred.
Frank
J
J
Department of Biomedical Sciences, Wadsworth Center, Albany, New York, 12201-0509, USA.
D001426:Bacterial Proteins / Q000378:metabolism / Q000648:ultrastructure; D001665:Binding Sites; D020285:Cryoelectron Microscopy / Q000379:methods; D004926:Escherichia coli / Q000378:metabolism / Q000648:ultrastructure; D008024:Ligands; D008961:Models, Structural; D012329:RNA, Bacterial / Q000378:metabolism / Q000648:ultrastructure; D012335:RNA, Ribosomal / Q000378:metabolism / Q000648:ultrastructure; D012269:Ribosomal Proteins / Q000378:metabolism / Q000648:ultrastructure; D012270:Ribosomes / Q000378:metabolism* / Q000648:ultrastructure*
D001426:Bacterial Proteins; D008024:Ligands; D012329:RNA, Bacterial; D012335:RNA, Ribosomal; D012269:Ribosomal Proteins