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1jke

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{{STRUCTURE_1jke| PDB=1jke | SCENE= }}
{{STRUCTURE_1jke| PDB=1jke | SCENE= }}
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'''D-Tyr tRNATyr deacylase from Escherichia coli'''
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===D-Tyr tRNATyr deacylase from Escherichia coli===
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==Overview==
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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.
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The line below this paragraph, {{ABSTRACT_PUBMED_11568181}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 11568181 is the PubMed ID number.
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{{ABSTRACT_PUBMED_11568181}}
==About this Structure==
==About this Structure==
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[[Category: Soutourina, J.]]
[[Category: Soutourina, J.]]
[[Category: Beta-alpha-barrel]]
[[Category: Beta-alpha-barrel]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 21:19:47 2008''
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Revision as of 17:22, 1 July 2008

Image:1jke.png

Template:STRUCTURE 1jke

D-Tyr tRNATyr deacylase from Escherichia coli

Template:ABSTRACT PUBMED 11568181

About this Structure

1JKE is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.

Reference

Structure of crystalline D-Tyr-tRNA(Tyr) deacylase. A representative of a new class of tRNA-dependent hydrolases., Ferri-Fioni ML, Schmitt E, Soutourina J, Plateau P, Mechulam Y, Blanquet S, J Biol Chem. 2001 Dec 14;276(50):47285-90. Epub 2001 Sep 21. PMID:11568181

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