1i9v | pdb_00001i9v

CRYSTAL STRUCTURE ANALYSIS OF A TRNA-NEOMYCIN COMPLEX

spinqualitylabelsall models 1i9v, resolution 2.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1i9v is a 1 chain structure with sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: MG, NMY NonStd Res: 5MU, YG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum Publication Abstract from PubMed Aminoglycosides bind to RNA and interfere with its function, and it has been suggested that aminoglycoside binding to RNA displaces essential divalent metal ions. Here we demonstrate that addition of various aminoglycosides inhibited Pb2+-induced cleavage of yeast tRNA(Phe). Cocrystallization of yeast tRNA(Phe) and an aminoglycoside, neomycin B, resulted in crystals that diffracted to 2.6 A and the structure of the complex was solved by molecular replacement. The structure shows that the neomycin B binding site overlaps with known divalent metal ion binding sites in yeast tRNA(Phe), providing direct evidence for the hypothesis that aminoglycosides displace metal ions. Additionally, the neomycin B binding site overlaps with major determinants for Escherichia coli phenylalanyl-tRNA-synthetase. Here we present data demonstrating that addition of neomycin B inhibited aminoacylation of E. coli tRNA(Phe) in the mid microM range. Given that aminoglycoside and metal ion binding sites overlap, we discuss that aminoglycosides can be considered as 'metal mimics'. Aminoglycoside binding displaces a divalent metal ion in a tRNA-neomycin B complex.,Mikkelsen NE, Johansson K, Virtanen A, Kirsebom LA Nat Struct Biol. 2001 Jun;8(6):510-4. PMID:11373618 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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