1jke
From Proteopedia
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- | [[Image:1jke.gif|left|200px]] | + | [[Image:1jke.gif|left|200px]] |
- | + | ||
- | '''D-Tyr tRNATyr deacylase from Escherichia coli''' | + | {{Structure |
+ | |PDB= 1jke |SIZE=350|CAPTION= <scene name='initialview01'>1jke</scene>, resolution 1.55Å | ||
+ | |SITE= | ||
+ | |LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene> | ||
+ | |ACTIVITY= | ||
+ | |GENE= YIHZ or B3887 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 Escherichia coli]) | ||
+ | }} | ||
+ | |||
+ | '''D-Tyr tRNATyr deacylase from Escherichia coli''' | ||
+ | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
- | 1JKE is a [ | + | 1JKE is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JKE OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11568181 11568181] |
[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: beta-alpha-barrel]] | [[Category: beta-alpha-barrel]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:04:35 2008'' |
Revision as of 10:04, 20 March 2008
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, resolution 1.55Å | |||||||
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Ligands: | |||||||
Gene: | YIHZ or B3887 (Escherichia coli) | ||||||
Coordinates: | save as pdb, mmCIF, xml |
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. 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
Page seeded by OCA on Thu Mar 20 12:04:35 2008