The structural basis of large ribosomal subunit function.
The ribosome crystal structures published in the past two years have revolutionized our understanding of ribonucleoprotein structure, and more specifically, the structural basis of the peptide bonding forming activity of the ribosome. This review concentrates on the crystallographic developments that made it possible to solve these structures. It also discusses the information obtained from these structures about the three-dimensional architecture of the large ribosomal subunit, the mechanism by which it facilitates peptide bond formation, and the way antibiotics inhibit large subunit function. The work reviewed, taken as a whole, proves beyond doubt that the ribosome is an RNA enzyme, as had long been surmised on the basis of less conclusive evidence.
Moore
Peter B
PB
Departments of Molecular Biophysics and Biochemistry, Chemistry, Yale University, New Haven, Connecticut 06520, USA. moore@proton.chem.yale
Steitz
Thomas A
TA
D019843:Archaeal Proteins / Q000737:chemistry / Q000378:metabolism; D001426:Bacterial Proteins / Q000737:chemistry / Q000378:metabolism; D018360:Crystallography, X-Ray; D008958:Models, Molecular; D009690:Nucleic Acid Conformation; D011487:Protein Conformation; D019642:RNA, Archaeal / Q000737:chemistry; D012329:RNA, Bacterial / Q000737:chemistry; D012335:RNA, Ribosomal / Q000037:antagonists & inhibitors / Q000737:chemistry* / Q000378:metabolism*; D012269:Ribosomal Proteins / Q000737:chemistry*; D012270:Ribosomes / Q000737:chemistry*
D019843:Archaeal Proteins; D001426:Bacterial Proteins; D019642:RNA, Archaeal; D012329:RNA, Bacterial; D012335:RNA, Ribosomal; D012269:Ribosomal Proteins