1y2q: Difference between revisions

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[[Image:1y2q.gif|left|200px]]<br /><applet load="1y2q" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1y2q.gif|left|200px]]<br /><applet load="1y2q" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1y2q, resolution 1.95Å" />

'''Crystal structure of the editing domain of threonyl-tRNA synthetase from Pyrococcus abyssi'''<br />

==Overview==

We report the crystal structure of an archaea-specific editing domain of, threonyl-tRNA synthetase that reveals a marked structural similarity to, D-amino acid deacylases found in eubacteria and eukaryotes. The domain can, bind D-amino acids despite a low sequence identity to other D-amino acid, deacylases. These results together indicate the presence of these, deacylases in all three kingdoms of life. This underlines an important, role they may have played in enforcing homochirality during translation.

We report the crystal structure of an archaea-specific editing domain of threonyl-tRNA synthetase that reveals a marked structural similarity to D-amino acid deacylases found in eubacteria and eukaryotes. The domain can bind D-amino acids despite a low sequence identity to other D-amino acid deacylases. These results together indicate the presence of these deacylases in all three kingdoms of life. This underlines an important role they may have played in enforcing homochirality during translation.

==About this Structure==

1Y2Q is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pyrococcus_abyssi Pyrococcus abyssi]. 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://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1Y2Q OCA].

1Y2Q is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pyrococcus_abyssi Pyrococcus abyssi]. 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=1Y2Q OCA].

==Reference==

Line 15:

[[Category: Threonine--tRNA ligase]]

[[Category: Dwivedi, S.]]

[[Category: Kruparani, S.P.]]

[[Category: Kruparani, S P.]]

[[Category: Sankaranarayanan, R.]]

[[Category: beta-alpha-beta fold]]

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[[Category: trna-synthetase]]

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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:01:14 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1y2q.gif|left|200px]]<br /><applet load="1y2q" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1y2q.gif|left|200px]]<br /><applet load="1y2q" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1y2q, resolution 1.95&Aring;" />
 '''Crystal structure of the editing domain of threonyl-tRNA synthetase from Pyrococcus abyssi'''<br />
 ==Overview==
-We report the crystal structure of an archaea-specific editing domain of, threonyl-tRNA synthetase that reveals a marked structural similarity to, D-amino acid deacylases found in eubacteria and eukaryotes. The domain can, bind D-amino acids despite a low sequence identity to other D-amino acid, deacylases. These results together indicate the presence of these, deacylases in all three kingdoms of life. This underlines an important, role they may have played in enforcing homochirality during translation.
+We report the crystal structure of an archaea-specific editing domain of threonyl-tRNA synthetase that reveals a marked structural similarity to D-amino acid deacylases found in eubacteria and eukaryotes. The domain can bind D-amino acids despite a low sequence identity to other D-amino acid deacylases. These results together indicate the presence of these deacylases in all three kingdoms of life. This underlines an important role they may have played in enforcing homochirality during translation.
 ==About this Structure==
-Y2Q is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pyrococcus_abyssi Pyrococcus abyssi]. 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1Y2Q OCA].
+Y2Q is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Pyrococcus_abyssi Pyrococcus abyssi]. 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=1Y2Q OCA].
 ==Reference==
@@ Line 15: / Line 15: @@
 [[Category: Threonine--tRNA ligase]]
 [[Category: Dwivedi, S.]]
-[[Category: Kruparani, S.P.]]
+[[Category: Kruparani, S P.]]
 [[Category: Sankaranarayanan, R.]]
 [[Category: beta-alpha-beta fold]]
@@ Line 21: / Line 21: @@
 [[Category: trna-synthetase]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 06:31:21 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:01:14 2008''