1JKE: D-Tyr Trnatyr Deacylase From Escherichia Coli

Citation:
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.
PDB ID: 1JKEDownload
MMDB ID: 18481
PDB Deposition Date: 2001/7/12
Updated in MMDB: 2011/11
Experimental Method:
x-ray diffraction
Resolution: 1.55  Å
Source Organism:
Similar Structures:
Biological Unit for 1JKE: dimeric; determined by author and by software (PISA)
Molecular Components in 1JKE
Label Count Molecule
Proteins (2 molecules)
2
D-tyr-trnatyr Deacylase(Gene symbol: dtd)
Molecule annotation
Chemicals (9 molecules)
1
9
* Click molecule labels to explore molecular sequence information.

Citing MMDB
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