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1i9v
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(New page: 200px<br /><applet load="1i9v" size="450" color="white" frame="true" align="right" spinBox="true" caption="1i9v, resolution 2.6Å" /> '''CRYSTAL STRUCTURE ANA...)
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Revision as of 01:42, 25 November 2007
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CRYSTAL STRUCTURE ANALYSIS OF A TRNA-NEOMYCIN COMPLEX
Overview
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'.
About this Structure
1I9V is a Single protein structure of sequence from Saccharomyces cerevisiae with MG and NMY as ligands. Full crystallographic information is available from OCA.
Reference
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
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