1fyf

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[[Image:1fyf.gif|left|200px]]<br /><applet load="1fyf" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1fyf.gif|left|200px]]
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caption="1fyf, resolution 1.65&Aring;" />
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'''CRYSTAL STRUCTURE OF A TRUNCATED FORM OF THREONYL-TRNA SYNTHETASE COMPLEXED WITH A SERYL ADENYLATE ANALOG'''<br />
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{{Structure
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|PDB= 1fyf |SIZE=350|CAPTION= <scene name='initialview01'>1fyf</scene>, resolution 1.65&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> and <scene name='pdbligand=SSA:5'-O-(N-(L-SERYL)-SULFAMOYL)ADENOSINE'>SSA</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Threonine--tRNA_ligase Threonine--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.3 6.1.1.3]
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|GENE=
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}}
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'''CRYSTAL STRUCTURE OF A TRUNCATED FORM OF THREONYL-TRNA SYNTHETASE COMPLEXED WITH A SERYL ADENYLATE ANALOG'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1FYF 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> and <scene name='pdbligand=SSA:'>SSA</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Threonine--tRNA_ligase Threonine--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.3 6.1.1.3] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FYF OCA].
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1FYF 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=1FYF OCA].
==Reference==
==Reference==
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Transfer RNA-mediated editing in threonyl-tRNA synthetase. The class II solution to the double discrimination problem., Dock-Bregeon A, Sankaranarayanan R, Romby P, Caillet J, Springer M, Rees B, Francklyn CS, Ehresmann C, Moras D, Cell. 2000 Dec 8;103(6):877-84. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11136973 11136973]
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Transfer RNA-mediated editing in threonyl-tRNA synthetase. The class II solution to the double discrimination problem., Dock-Bregeon A, Sankaranarayanan R, Romby P, Caillet J, Springer M, Rees B, Francklyn CS, Ehresmann C, Moras D, Cell. 2000 Dec 8;103(6):877-84. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11136973 11136973]
[[Category: Escherichia coli]]
[[Category: Escherichia coli]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: zinc ion]]
[[Category: zinc ion]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:43:58 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:15:38 2008''

Revision as of 09:15, 20 March 2008


PDB ID 1fyf

Drag the structure with the mouse to rotate
, resolution 1.65Å
Ligands: and
Activity: Threonine--tRNA ligase, with EC number 6.1.1.3
Coordinates: save as pdb, mmCIF, xml



CRYSTAL STRUCTURE OF A TRUNCATED FORM OF THREONYL-TRNA SYNTHETASE COMPLEXED WITH A SERYL ADENYLATE ANALOG


Overview

Threonyl-tRNA synthetase, a class II synthetase, uses a unique zinc ion to discriminate against the isosteric valine at the activation step. The crystal structure of the enzyme with an analog of seryl adenylate shows that the noncognate serine cannot be fully discriminated at that step. We show that hydrolysis of the incorrectly formed ser-tRNA(Thr) is performed at a specific site in the N-terminal domain of the enzyme. The present study suggests that both classes of synthetases use effectively the ability of the CCA end of tRNA to switch between a hairpin and a helical conformation for aminoacylation and editing. As a consequence, the editing mechanism of both classes of synthetases can be described as mirror images, as already seen for tRNA binding and amino acid activation.

About this Structure

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

Reference

Transfer RNA-mediated editing in threonyl-tRNA synthetase. The class II solution to the double discrimination problem., Dock-Bregeon A, Sankaranarayanan R, Romby P, Caillet J, Springer M, Rees B, Francklyn CS, Ehresmann C, Moras D, Cell. 2000 Dec 8;103(6):877-84. PMID:11136973

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