PMID:11568181
| Citation |
Ferri-Fioni, ML, Schmitt, E, Soutourina, J, Plateau, P, Mechulam, Y and Blanquet, S (2001) Structure of crystalline D-Tyr-tRNA(Tyr) deacylase. A representative of a new class of tRNA-dependent hydrolases. J. Biol. Chem. 276:47285-90 |
|---|---|
| Abstract |
Cell growth inhibition by several d-amino acids can be explained by an in vivo production of d-aminoacyl-tRNA molecules. Escherichia coli and yeast cells express an enzyme, d-Tyr-tRNA(Tyr) deacylase, capable of recycling such d-aminoacyl-tRNA molecules into free tRNA and d-amino acid. Accordingly, upon inactivation of the genes of the above deacylases, the toxicity of d-amino acids increases. Orthologs of the deacylase are found in many cells. In this study, the crystallographic structure of dimeric E. coli d-Tyr-tRNA(Tyr) deacylase at 1.55 A resolution is reported. The structure corresponds to a beta-barrel closed on one side by a beta-sheet lid. This barrel results from the assembly of the two subunits. Analysis of the structure in relation with sequence homologies in the orthologous family suggests the location of the active sites at the carboxy end of the beta-strands. The solved structure markedly differs from those of all other documented tRNA-dependent hydrolases. |
| Links |
PubMed Online version:10.1074/jbc.M106550200 |
| Keywords |
Amino Acid Sequence; Aminoacyltransferases/chemistry; Aminoacyltransferases/classification; Binding Sites; Cell Division; Crystallography, X-Ray; Dimerization; Escherichia coli/enzymology; Ions; Ligands; Models, Biological; Models, Molecular; Models, Statistical; Molecular Sequence Data; Protein Structure, Secondary; RNA, Transfer/metabolism; Spectrophotometry, Atomic; Zinc/chemistry |
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