1iyw
From Proteopedia
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- | [[Image:1iyw.jpg|left|200px]] | + | [[Image:1iyw.jpg|left|200px]] |
- | + | ||
- | '''Preliminary Structure of Thermus thermophilus Ligand-Free Valyl-tRNA Synthetase''' | + | {{Structure |
+ | |PDB= 1iyw |SIZE=350|CAPTION= <scene name='initialview01'>1iyw</scene>, resolution 4.0Å | ||
+ | |SITE= | ||
+ | |LIGAND= | ||
+ | |ACTIVITY= [http://en.wikipedia.org/wiki/Valine--tRNA_ligase Valine--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.9 6.1.1.9] | ||
+ | |GENE= | ||
+ | }} | ||
+ | |||
+ | '''Preliminary Structure of Thermus thermophilus Ligand-Free Valyl-tRNA Synthetase''' | ||
+ | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
- | 1IYW is a [ | + | 1IYW 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=1IYW OCA]. |
==Reference== | ==Reference== | ||
- | Mechanism of molecular interactions for tRNA(Val) recognition by valyl-tRNA synthetase., Fukai S, Nureki O, Sekine S, Shimada A, Vassylyev DG, Yokoyama S, RNA. 2003 Jan;9(1):100-11. PMID:[http:// | + | Mechanism of molecular interactions for tRNA(Val) recognition by valyl-tRNA synthetase., Fukai S, Nureki O, Sekine S, Shimada A, Vassylyev DG, Yokoyama S, RNA. 2003 Jan;9(1):100-11. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12554880 12554880] |
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Thermus thermophilus]] | [[Category: Thermus thermophilus]] | ||
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[[Category: rossmann fold]] | [[Category: rossmann fold]] | ||
[[Category: rsgi]] | [[Category: rsgi]] | ||
- | [[Category: structural | + | [[Category: structural genomic]] |
- | ''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 11:56:46 2008'' |
Revision as of 09:56, 20 March 2008
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, resolution 4.0Å | |||||||
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Activity: | Valine--tRNA ligase, with EC number 6.1.1.9 | ||||||
Coordinates: | save as pdb, mmCIF, xml |
Preliminary Structure of Thermus thermophilus Ligand-Free Valyl-tRNA Synthetase
Overview
The molecular interactions between valyl-tRNA synthetase (ValRS) and tRNA(Val), with the C34-A35-C36 anticodon, from Thermus thermophilus were studied by crystallographic analysis and structure-based mutagenesis. In the ValRS-bound structure of tRNA(Val), the successive A35-C36 residues (the major identity elements) of tRNA(Val) are base-stacked upon each other, and fit into a pocket on the alpha-helix bundle domain of ValRS. Hydrogen bonds are formed between ValRS and A35-C36 of tRNA(Val) in a base-specific manner. The C-terminal coiled-coil domain of ValRS interacts electrostatically with A20 and hydrophobically with the G19*C56 tertiary base pair. The loss of these interactions by the deletion of the coiled-coil domain of ValRS increased the K(M) value for tRNA(Val) 28-fold and decreased the k(cat) value 19-fold in the aminoacylation. The tRNA(Val) K(M) and k(cat) values were increased 21-fold and decreased 32-fold, respectively, by the disruption of the G18*U55 and G19*C56 tertiary base pairs, which associate the D- and T-loops for the formation of the L-shaped tRNA structure. Therefore, the coiled-coil domain of ValRS is likely to stabilize the L-shaped tRNA structure during the aminoacylation reaction.
About this Structure
1IYW is a Single protein structure of sequence from Thermus thermophilus. Full crystallographic information is available from OCA.
Reference
Mechanism of molecular interactions for tRNA(Val) recognition by valyl-tRNA synthetase., Fukai S, Nureki O, Sekine S, Shimada A, Vassylyev DG, Yokoyama S, RNA. 2003 Jan;9(1):100-11. PMID:12554880
Page seeded by OCA on Thu Mar 20 11:56:46 2008
Categories: Single protein | Thermus thermophilus | Valine--tRNA ligase | Fukai, S. | Nureki, O. | RSGI, RIKEN Structural Genomics/Proteomics Initiative. | Sekine, S. | Shimada, A. | Vassylyev, D G. | Yokoyama, S. | Coiled coil | Riken structural genomics/proteomics initiative | Rossmann fold | Rsgi | Structural genomic