On the structural basis of peptide-bond formation and antibiotic resistance from atomic structures of the large ribosomal subunit.
The atomic structures of the large ribosomal subunit from Haloarcula marismortui and its complexes with substrates and antibiotics have provided insights into the way the 3000 nucleotide 23S rRNA folds into a compact, specific structure and interacts with 27 ribosomal proteins as well as the structural basis of the peptidyl transferase reaction and its inhibition by antibiotics. The structure shows that the ribosome is indeed a ribozyme.
Steitz
Thomas A
TA
Department of Molecular Biophysics and Biochemistry, Yale University, and Howard Hughes Medical Institute, P.O. Box 208114, New Haven, CT 06520-8114, USA. eatherton@csb.yale.edu
D000900:Anti-Bacterial Agents / Q000737:chemistry* / Q000494:pharmacology; D004352:Drug Resistance, Microbial; D019614:Haloarcula marismortui / Q000502:physiology; D015394:Molecular Structure; D009690:Nucleic Acid Conformation; D010441:Peptide Chain Elongation, Translational / Q000187:drug effects / Q000502:physiology; D010458:Peptidyl Transferases / Q000502:physiology; D014176:Protein Biosynthesis / Q000187:drug effects; D012338:RNA, Ribosomal, 23S / Q000378:metabolism; D012343:RNA, Transfer / Q000378:metabolism; D012269:Ribosomal Proteins / Q000737:chemistry / Q000502:physiology; D012270:Ribosomes / Q000737:chemistry* / Q000187:drug effects*
D000900:Anti-Bacterial Agents; D012338:RNA, Ribosomal, 23S; D012269:Ribosomal Proteins; D012343:RNA, Transfer; D010458:Peptidyl Transferases