1g59

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(New page: 200px<br /><applet load="1g59" size="450" color="white" frame="true" align="right" spinBox="true" caption="1g59, resolution 2.4&Aring;" /> '''GLUTAMYL-TRNA SYNTHET...)
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[[Image:1g59.gif|left|200px]]<br /><applet load="1g59" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1g59, resolution 2.4&Aring;" />
caption="1g59, resolution 2.4&Aring;" />
'''GLUTAMYL-TRNA SYNTHETASE COMPLEXED WITH TRNA(GLU).'''<br />
'''GLUTAMYL-TRNA SYNTHETASE COMPLEXED WITH TRNA(GLU).'''<br />
==Overview==
==Overview==
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Glutamyl-tRNA synthetases (GluRSs) are divided into two distinct types, with regard to the presence or absence of glutaminyl-tRNA synthetase, (GlnRS) in the genetic translation systems. In the original 19-synthetase, systems lacking GlnRS, the 'non-discriminating' GluRS glutamylates both, tRNAGlu and tRNAGln. In contrast, in the evolved 20-synthetase systems, with GlnRS, the 'discriminating' GluRS aminoacylates only tRNAGlu. Here we, report the 2.4 A resolution crystal structure of a 'discriminating', GluRS.tRNAGlu complex from Thermus thermophilus. The GluRS recognizes the, tRNAGlu anticodon bases via two alpha-helical domains, maintaining the, base stacking. We show that the discrimination between the Glu and Gln, anticodons (34YUC36 and 34YUG36, respectively) is achieved by a single, arginine residue (Arg 358). The mutation of Arg 358 to Gln resulted in a, GluRS that does not discriminate between the Glu and Gln anticodons. This, change mimics the reverse course of GluRS evolution from anticodon, 'non-dicsriminating' to 'discriminating'.
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Glutamyl-tRNA synthetases (GluRSs) are divided into two distinct types, with regard to the presence or absence of glutaminyl-tRNA synthetase (GlnRS) in the genetic translation systems. In the original 19-synthetase systems lacking GlnRS, the 'non-discriminating' GluRS glutamylates both tRNAGlu and tRNAGln. In contrast, in the evolved 20-synthetase systems with GlnRS, the 'discriminating' GluRS aminoacylates only tRNAGlu. Here we report the 2.4 A resolution crystal structure of a 'discriminating' GluRS.tRNAGlu complex from Thermus thermophilus. The GluRS recognizes the tRNAGlu anticodon bases via two alpha-helical domains, maintaining the base stacking. We show that the discrimination between the Glu and Gln anticodons (34YUC36 and 34YUG36, respectively) is achieved by a single arginine residue (Arg 358). The mutation of Arg 358 to Gln resulted in a GluRS that does not discriminate between the Glu and Gln anticodons. This change mimics the reverse course of GluRS evolution from anticodon 'non-dicsriminating' to 'discriminating'.
==About this Structure==
==About this Structure==
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1G59 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Active as [http://en.wikipedia.org/wiki/Glutamate--tRNA_ligase Glutamate--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.17 6.1.1.17] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1G59 OCA].
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1G59 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Active as [http://en.wikipedia.org/wiki/Glutamate--tRNA_ligase Glutamate--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.17 6.1.1.17] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G59 OCA].
==Reference==
==Reference==
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[[Category: Thermus thermophilus]]
[[Category: Thermus thermophilus]]
[[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: Sekine, S.]]
[[Category: Sekine, S.]]
[[Category: Shimada, A.]]
[[Category: Shimada, A.]]
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[[Category: Vassylyev, D.G.]]
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[[Category: Vassylyev, D G.]]
[[Category: Yokoyama, S.]]
[[Category: Yokoyama, S.]]
[[Category: aminoacyl-trna synthetase]]
[[Category: aminoacyl-trna synthetase]]
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[[Category: transfer rna]]
[[Category: transfer rna]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 15:43:04 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:46:13 2008''

Revision as of 10:46, 21 February 2008


1g59, resolution 2.4Å

Drag the structure with the mouse to rotate

GLUTAMYL-TRNA SYNTHETASE COMPLEXED WITH TRNA(GLU).

Overview

Glutamyl-tRNA synthetases (GluRSs) are divided into two distinct types, with regard to the presence or absence of glutaminyl-tRNA synthetase (GlnRS) in the genetic translation systems. In the original 19-synthetase systems lacking GlnRS, the 'non-discriminating' GluRS glutamylates both tRNAGlu and tRNAGln. In contrast, in the evolved 20-synthetase systems with GlnRS, the 'discriminating' GluRS aminoacylates only tRNAGlu. Here we report the 2.4 A resolution crystal structure of a 'discriminating' GluRS.tRNAGlu complex from Thermus thermophilus. The GluRS recognizes the tRNAGlu anticodon bases via two alpha-helical domains, maintaining the base stacking. We show that the discrimination between the Glu and Gln anticodons (34YUC36 and 34YUG36, respectively) is achieved by a single arginine residue (Arg 358). The mutation of Arg 358 to Gln resulted in a GluRS that does not discriminate between the Glu and Gln anticodons. This change mimics the reverse course of GluRS evolution from anticodon 'non-dicsriminating' to 'discriminating'.

About this Structure

1G59 is a Single protein structure of sequence from Thermus thermophilus. Active as Glutamate--tRNA ligase, with EC number 6.1.1.17 Full crystallographic information is available from OCA.

Reference

Structural basis for anticodon recognition by discriminating glutamyl-tRNA synthetase., Sekine S, Nureki O, Shimada A, Vassylyev DG, Yokoyama S, Nat Struct Biol. 2001 Mar;8(3):203-6. PMID:11224561

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