Structure of crystalline D-Tyr-tRNA(Tyr) deacylase. A representative of a new class of tRNA-dependent hydrolases

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, u...

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Bibliographic Details
Published in:The Journal of biological chemistry 2001-12, Vol.276 (50), p.47285-47290
Main Authors: Ferri-Fioni, M L, Schmitt, E, Soutourina, J, Plateau, P, Mechulam, Y, Blanquet, S
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Aminoacyltransferases
Aminoacyltransferases - chemistry
Aminoacyltransferases - classification
Binding Sites
Biochemistry, Molecular Biology
Cell Division
Crystallography, X-Ray
Dimerization
Escherichia coli
Escherichia coli - enzymology
Ions
Life Sciences
Ligands
Models, Biological
Models, Molecular
Models, Statistical
Molecular Sequence Data
Protein Structure, Secondary
RNA, Transfer
RNA, Transfer - metabolism
Spectrophotometry, Atomic
Zinc
Zinc - chemistry
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Summary: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.
ISSN:0021-9258
1083-351X
DOI:10.1074/jbc.M106550200