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1g59
From Proteopedia
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| - | [[Image:1g59.gif|left|200px]] | + | [[Image:1g59.gif|left|200px]] |
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| - | '''GLUTAMYL-TRNA SYNTHETASE COMPLEXED WITH TRNA(GLU).''' | + | {{Structure |
| + | |PDB= 1g59 |SIZE=350|CAPTION= <scene name='initialview01'>1g59</scene>, resolution 2.4Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= [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] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''GLUTAMYL-TRNA SYNTHETASE COMPLEXED WITH TRNA(GLU).''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1G59 is a [ | + | 1G59 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Thermus_thermophilus Thermus thermophilus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G59 OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11224561 11224561] |
[[Category: Glutamate--tRNA ligase]] | [[Category: Glutamate--tRNA ligase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: riken structural genomics/proteomics initiative]] | [[Category: riken structural genomics/proteomics initiative]] | ||
[[Category: rsgi]] | [[Category: rsgi]] | ||
| - | [[Category: structural | + | [[Category: structural genomic]] |
[[Category: transfer rna]] | [[Category: transfer rna]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:18:21 2008'' |
Revision as of 09:18, 20 March 2008
| |||||||
| , resolution 2.4Å | |||||||
|---|---|---|---|---|---|---|---|
| Activity: | Glutamate--tRNA ligase, with EC number 6.1.1.17 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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
Page seeded by OCA on Thu Mar 20 11:18:21 2008
Categories: Glutamate--tRNA ligase | Single protein | Thermus thermophilus | Nureki, O. | RSGI, RIKEN Structural Genomics/Proteomics Initiative. | Sekine, S. | Shimada, A. | Vassylyev, D G. | Yokoyama, S. | Aminoacyl-trna synthetase | Protein-rna complex | Riken structural genomics/proteomics initiative | Rsgi | Structural genomic | Transfer rna
