1jke

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(New page: 200px<br /><applet load="1jke" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jke, resolution 1.55&Aring;" /> '''D-Tyr tRNATyr deacyl...)
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[[Image:1jke.gif|left|200px]]<br /><applet load="1jke" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1jke.gif|left|200px]]<br /><applet load="1jke" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1jke, resolution 1.55&Aring;" />
caption="1jke, resolution 1.55&Aring;" />
'''D-Tyr tRNATyr deacylase from Escherichia coli'''<br />
'''D-Tyr tRNATyr deacylase from Escherichia coli'''<br />
==Overview==
==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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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.
==About this Structure==
==About this Structure==
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1JKE is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with ZN as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1JKE OCA].
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1JKE is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JKE OCA].
==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Blanquet, S.]]
[[Category: Blanquet, S.]]
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[[Category: Ferri-Fioni, M.L.]]
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[[Category: Ferri-Fioni, M L.]]
[[Category: Mechulam, Y.]]
[[Category: Mechulam, Y.]]
[[Category: Plateau, P.]]
[[Category: Plateau, P.]]
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[[Category: beta-alpha-barrel]]
[[Category: beta-alpha-barrel]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 18:20:36 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:23:37 2008''

Revision as of 11:23, 21 February 2008


1jke, resolution 1.55Å

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D-Tyr tRNATyr deacylase from Escherichia coli

Overview

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.

About this Structure

1JKE is a Single protein structure of sequence from Escherichia coli with as ligand. 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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