1j1u

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(New page: 200px<br /><applet load="1j1u" size="450" color="white" frame="true" align="right" spinBox="true" caption="1j1u, resolution 1.95&Aring;" /> '''Crystal structure of...)
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[[Image:1j1u.gif|left|200px]]<br /><applet load="1j1u" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1j1u.gif|left|200px]]<br /><applet load="1j1u" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1j1u, resolution 1.95&Aring;" />
caption="1j1u, resolution 1.95&Aring;" />
'''Crystal structure of archaeal tyrosyl-tRNA synthetase complexed with tRNA(Tyr) and L-tyrosine'''<br />
'''Crystal structure of archaeal tyrosyl-tRNA synthetase complexed with tRNA(Tyr) and L-tyrosine'''<br />
==Overview==
==Overview==
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The archaeal/eukaryotic tyrosyl-tRNA synthetase (TyrRS)-tRNA(Tyr) pairs do, not cross-react with their bacterial counterparts. This 'orthogonal', condition is essential for using the archaeal pair to expand the bacterial, genetic code. In this study, the structure of the Methanococcus jannaschii, TyrRS-tRNA(Tyr)-L-tyrosine complex, solved at a resolution of 1.95 A, reveals that this archaeal TyrRS strictly recognizes the C1-G72 base pair, whereas the bacterial TyrRS recognizes the G1-C72 in a different manner, using different residues. These diverse tRNA recognition modes form the, basis for the orthogonality. The common tRNA(Tyr) identity determinants, (the discriminator, A73 and the anticodon residues) are also recognized in, manners different from those of the bacterial TyrRS. Based on this, finding, we created a mutant TyrRS that aminoacylates the amber suppressor, tRNA with C34 65 times more efficiently than does the wild-type enzyme.
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The archaeal/eukaryotic tyrosyl-tRNA synthetase (TyrRS)-tRNA(Tyr) pairs do not cross-react with their bacterial counterparts. This 'orthogonal' condition is essential for using the archaeal pair to expand the bacterial genetic code. In this study, the structure of the Methanococcus jannaschii TyrRS-tRNA(Tyr)-L-tyrosine complex, solved at a resolution of 1.95 A, reveals that this archaeal TyrRS strictly recognizes the C1-G72 base pair, whereas the bacterial TyrRS recognizes the G1-C72 in a different manner using different residues. These diverse tRNA recognition modes form the basis for the orthogonality. The common tRNA(Tyr) identity determinants (the discriminator, A73 and the anticodon residues) are also recognized in manners different from those of the bacterial TyrRS. Based on this finding, we created a mutant TyrRS that aminoacylates the amber suppressor tRNA with C34 65 times more efficiently than does the wild-type enzyme.
==About this Structure==
==About this Structure==
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1J1U 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 MG and TYR 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1J1U OCA].
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1J1U 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=MG:'>MG</scene> and <scene name='pdbligand=TYR:'>TYR</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=1J1U OCA].
==Reference==
==Reference==
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[[Category: Kobayashi, T.]]
[[Category: Kobayashi, T.]]
[[Category: Nureki, O.]]
[[Category: Nureki, O.]]
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[[Category: RSGI, RIKEN.Structural.Genomics/Proteomics.Initiative.]]
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[[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]]
[[Category: Sakamoto, K.]]
[[Category: Sakamoto, K.]]
[[Category: Tukalo, M.]]
[[Category: Tukalo, M.]]
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[[Category: trna]]
[[Category: trna]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 17:52:05 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:18:02 2008''

Revision as of 11:18, 21 February 2008


1j1u, resolution 1.95Å

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Crystal structure of archaeal tyrosyl-tRNA synthetase complexed with tRNA(Tyr) and L-tyrosine

Overview

The archaeal/eukaryotic tyrosyl-tRNA synthetase (TyrRS)-tRNA(Tyr) pairs do not cross-react with their bacterial counterparts. This 'orthogonal' condition is essential for using the archaeal pair to expand the bacterial genetic code. In this study, the structure of the Methanococcus jannaschii TyrRS-tRNA(Tyr)-L-tyrosine complex, solved at a resolution of 1.95 A, reveals that this archaeal TyrRS strictly recognizes the C1-G72 base pair, whereas the bacterial TyrRS recognizes the G1-C72 in a different manner using different residues. These diverse tRNA recognition modes form the basis for the orthogonality. The common tRNA(Tyr) identity determinants (the discriminator, A73 and the anticodon residues) are also recognized in manners different from those of the bacterial TyrRS. Based on this finding, we created a mutant TyrRS that aminoacylates the amber suppressor tRNA with C34 65 times more efficiently than does the wild-type enzyme.

About this Structure

1J1U is a Single protein structure of sequence from Methanocaldococcus jannaschii with and as ligands. Active as Tyrosine--tRNA ligase, with EC number 6.1.1.1 Full crystallographic information is available from OCA.

Reference

Structural basis for orthogonal tRNA specificities of tyrosyl-tRNA synthetases for genetic code expansion., Kobayashi T, Nureki O, Ishitani R, Yaremchuk A, Tukalo M, Cusack S, Sakamoto K, Yokoyama S, Nat Struct Biol. 2003 Jun;10(6):425-32. PMID:12754495

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