1n3l

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[[Image:1n3l.jpg|left|200px]]<br /><applet load="1n3l" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1n3l.jpg|left|200px]]
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caption="1n3l, resolution 1.18&Aring;" />
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'''Crystal structure of a human aminoacyl-tRNA synthetase cytokine'''<br />
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{{Structure
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|PDB= 1n3l |SIZE=350|CAPTION= <scene name='initialview01'>1n3l</scene>, resolution 1.18&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Tyrosine--tRNA_ligase Tyrosine--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.1 6.1.1.1]
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|GENE=
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}}
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'''Crystal structure of a human aminoacyl-tRNA synthetase cytokine'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1N3L is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Tyrosine--tRNA_ligase Tyrosine--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.1 6.1.1.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N3L OCA].
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1N3L is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N3L OCA].
==Reference==
==Reference==
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Crystal structure of a human aminoacyl-tRNA synthetase cytokine., Yang XL, Skene RJ, McRee DE, Schimmel P, Proc Natl Acad Sci U S A. 2002 Nov 26;99(24):15369-74. Epub 2002 Nov 11. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12427973 12427973]
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Crystal structure of a human aminoacyl-tRNA synthetase cytokine., Yang XL, Skene RJ, McRee DE, Schimmel P, Proc Natl Acad Sci U S A. 2002 Nov 26;99(24):15369-74. Epub 2002 Nov 11. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12427973 12427973]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: unique anticodon recognition domain]]
[[Category: unique anticodon recognition domain]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:01:55 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:51:41 2008''

Revision as of 10:51, 20 March 2008


PDB ID 1n3l

Drag the structure with the mouse to rotate
, resolution 1.18Å
Ligands: and
Activity: Tyrosine--tRNA ligase, with EC number 6.1.1.1
Coordinates: save as pdb, mmCIF, xml



Crystal structure of a human aminoacyl-tRNA synthetase cytokine


Contents

Overview

The 20 aminoacyl-tRNA synthetases catalyze the first step of protein synthesis and establish the rules of the genetic code through aminoacylation reactions. Biological fragments of two human enzymes, tyrosyl-tRNA synthetase (TyrRS) and tryptophanyl-tRNA synthetase, connect protein synthesis to cell-signaling pathways including angiogenesis. Alternative splicing or proteolysis produces these fragments. The proangiogenic N-terminal fragment mini-TyrRS has IL-8-like cytokine activity that, like other CXC cytokines, depends on a Glu-Leu-Arg motif. Point mutations in this motif abolish cytokine activity. The full-length native TyrRS lacks cytokine activity. No structure has been available for any mammalian tRNA synthetase that, in turn, might give insight into why mini-TyrRS and not TyrRS has cytokine activities. Here, the structure of human mini-TyrRS, which contains both the catalytic and the anticodon recognition domain, is reported to a resolution of 1.18 A. The critical Glu-Leu-Arg motif is located on an internal alpha-helix of the catalytic domain, where the guanidino side chain of R is part of a hydrogen-bonding network tethering the anticodon-recognition domain back to the catalytic site. Whereas the catalytic domains of the human and bacterial enzymes superimpose, the spatial disposition of the anticodon recognition domain relative to the catalytic domain is unique in mini-TyrRS relative to the bacterial orthologs. This unique orientation of the anticodon-recognition domain can explain why the fragment mini-TyrRS, and not full-length native TyrRS, is active in cytokine-signaling pathways.

Disease

Known disease associated with this structure: Charcot-Marie-Tooth disease, dominant intermediate C OMIM:[603623]

About this Structure

1N3L is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Crystal structure of a human aminoacyl-tRNA synthetase cytokine., Yang XL, Skene RJ, McRee DE, Schimmel P, Proc Natl Acad Sci U S A. 2002 Nov 26;99(24):15369-74. Epub 2002 Nov 11. PMID:12427973

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