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On the structural basis of peptide‐bond formation and antibiotic resistance from atomic structures of the large ribosomal subunit
Author(s) -
Steitz Thomas A.
Publication year - 2005
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2004.11.053
Subject(s) - ribosome , peptidyl transferase , ribosomal rna , 23s ribosomal rna , eukaryotic large ribosomal subunit , 50s , eukaryotic ribosome , ribozyme , protein subunit , chemistry , ribosomal protein , peptide bond , biochemistry , peptide , rna , gene
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.