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Inhibitors of the Large Ribosomal Subunit from Haloarcula marismortui
Author(s) -
Moore Peter B.
Publication year - 2010
Publication title -
israel journal of chemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.908
H-Index - 54
eISSN - 1869-5868
pISSN - 0021-2148
DOI - 10.1002/ijch.201000001
Subject(s) - chemistry , ribosomal rna , protein subunit , ribosomal protein , 50s , peptidyl transferase , eukaryotic large ribosomal subunit , biochemistry , stereochemistry , ribosome , 18s ribosomal rna , rna , gene
The crystal structures that have been obtained for 23 different inhibitors bound to the large ribosomal subunit from Haloarcula marismortui are reviewed here. These structures provide important insights into how anti‐ribosomal antibiotics inhibit protein synthesis, how species specificity arises, and the relationship between ribosomal mutations and antibiotic resistance. These structural studies also provide compelling evidence that the conformation of the peptidyl transferase center of the large ribosomal subunit is intrinsically variable, and that conformational equilibria play a role in determining its functional properties.