2ag6

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[[Image:2ag6.gif|left|200px]]<br /><applet load="2ag6" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2ag6.gif|left|200px]]
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caption="2ag6, resolution 1.90&Aring;" />
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'''Crystal structure of p-bromo-l-phenylalanine-tRNA sythetase in complex with p-bromo-l-phenylalanine'''<br />
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{{Structure
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|PDB= 2ag6 |SIZE=350|CAPTION= <scene name='initialview01'>2ag6</scene>, resolution 1.90&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=4BF:4-BROMO-L-PHENYLALANINE'>4BF</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= tyrS ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=2190 Methanocaldococcus jannaschii])
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}}
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'''Crystal structure of p-bromo-l-phenylalanine-tRNA sythetase in complex with p-bromo-l-phenylalanine'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2AG6 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii Methanocaldococcus jannaschii] with <scene name='pdbligand=4BF:'>4BF</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. 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=2AG6 OCA].
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2AG6 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Methanocaldococcus_jannaschii Methanocaldococcus jannaschii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2AG6 OCA].
==Reference==
==Reference==
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Structural plasticity of an aminoacyl-tRNA synthetase active site., Turner JM, Graziano J, Spraggon G, Schultz PG, Proc Natl Acad Sci U S A. 2006 Apr 25;103(17):6483-8. Epub 2006 Apr 17. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16618920 16618920]
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Structural plasticity of an aminoacyl-tRNA synthetase active site., Turner JM, Graziano J, Spraggon G, Schultz PG, Proc Natl Acad Sci U S A. 2006 Apr 25;103(17):6483-8. Epub 2006 Apr 17. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16618920 16618920]
[[Category: Methanocaldococcus jannaschii]]
[[Category: Methanocaldococcus jannaschii]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: unnatural amino acid]]
[[Category: unnatural amino acid]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:27:05 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:49:19 2008''

Revision as of 13:49, 20 March 2008


PDB ID 2ag6

Drag the structure with the mouse to rotate
, resolution 1.90Å
Ligands:
Gene: tyrS (Methanocaldococcus jannaschii)
Activity: Tyrosine--tRNA ligase, with EC number 6.1.1.1
Coordinates: save as pdb, mmCIF, xml



Crystal structure of p-bromo-l-phenylalanine-tRNA sythetase in complex with p-bromo-l-phenylalanine


Overview

Recently, tRNA aminoacyl-tRNA synthetase pairs have been evolved that allow one to genetically encode a large array of unnatural amino acids in both prokaryotic and eukaryotic organisms. We have determined the crystal structures of two substrate-bound Methanococcus jannaschii tyrosyl aminoacyl-tRNA synthetases that charge the unnatural amino acids p-bromophenylalanine and 3-(2-naphthyl)alanine (NpAla). A comparison of these structures with the substrate-bound WT synthetase, as well as a mutant synthetase that charges p-acetylphenylalanine, shows that altered specificity is due to both side-chain and backbone rearrangements within the active site that modify hydrogen bonds and packing interactions with substrate, as well as disrupt the alpha8-helix, which spans the WT active site. The high degree of structural plasticity that is observed in these aminoacyl-tRNA synthetases is rarely found in other mutant enzymes with altered specificities and provides an explanation for the surprising adaptability of the genetic code to novel amino acids.

About this Structure

2AG6 is a Single protein structure of sequence from Methanocaldococcus jannaschii. Full crystallographic information is available from OCA.

Reference

Structural plasticity of an aminoacyl-tRNA synthetase active site., Turner JM, Graziano J, Spraggon G, Schultz PG, Proc Natl Acad Sci U S A. 2006 Apr 25;103(17):6483-8. Epub 2006 Apr 17. PMID:16618920

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