1ue0
From Proteopedia
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| - | [[Image:1ue0.jpg|left|200px]] | + | [[Image:1ue0.jpg|left|200px]] |
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| - | '''Isoleucyl-tRNA synthetase editing domain complexed with L-Valine''' | + | {{Structure |
| + | |PDB= 1ue0 |SIZE=350|CAPTION= <scene name='initialview01'>1ue0</scene>, resolution 2.00Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=VAL:VALINE'>VAL</scene> | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Isoleucine--tRNA_ligase Isoleucine--tRNA ligase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=6.1.1.5 6.1.1.5] | ||
| + | |GENE= iles ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=274 Thermus thermophilus]) | ||
| + | }} | ||
| + | |||
| + | '''Isoleucyl-tRNA synthetase editing domain complexed with L-Valine''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1UE0 is a [ | + | 1UE0 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=1UE0 OCA]. |
==Reference== | ==Reference== | ||
| - | Crystal structures of the CP1 domain from Thermus thermophilus isoleucyl-tRNA synthetase and its complex with L-valine., Fukunaga R, Fukai S, Ishitani R, Nureki O, Yokoyama S, J Biol Chem. 2004 Feb 27;279(9):8396-402. Epub 2003 Dec 12. PMID:[http:// | + | Crystal structures of the CP1 domain from Thermus thermophilus isoleucyl-tRNA synthetase and its complex with L-valine., Fukunaga R, Fukai S, Ishitani R, Nureki O, Yokoyama S, J Biol Chem. 2004 Feb 27;279(9):8396-402. Epub 2003 Dec 12. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14672940 14672940] |
[[Category: Isoleucine--tRNA ligase]] | [[Category: Isoleucine--tRNA ligase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: cp1]] | [[Category: cp1]] | ||
[[Category: editing]] | [[Category: editing]] | ||
| - | [[Category: national project on protein structural and functional | + | [[Category: national project on protein structural and functional analyse]] |
[[Category: nppsfa]] | [[Category: nppsfa]] | ||
[[Category: riken structural genomics/proteomics initiative]] | [[Category: riken structural genomics/proteomics initiative]] | ||
[[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 14:30:46 2008'' |
Revision as of 12:30, 20 March 2008
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| , resolution 2.00Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | iles (Thermus thermophilus) | ||||||
| Activity: | Isoleucine--tRNA ligase, with EC number 6.1.1.5 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Isoleucyl-tRNA synthetase editing domain complexed with L-Valine
Overview
Isoleucyl-tRNA synthetase (IleRS) links tRNA(Ile) with not only its cognate isoleucine but also the nearly cognate valine. The CP1 domain of IleRS deacylates, or edits, the mischarged Val-tRNA(Ile). We determined the crystal structures of the Thermus thermophilus IleRS CP1 domain alone, and in its complex with valine at 1.8- and 2.0-A resolutions, respectively. In the complex structure, the Asp(328) residue, which was shown to be critical for the editing reaction against Val-tRNA(Ile) by a previous mutational analysis, recognizes the valine NH(3)(+) group. The valine side chain binding pocket is only large enough to accommodate valine, and the placement of an isoleucine model in this location revealed that the additional methylene group of isoleucine would clash with His(319). The H319A mutant of Escherichia coli IleRS reportedly deacylates the cognate Ile-tRNA(Ile) in addition to Val-tRNA(Ile), indicating that the valine-binding mode found in this study represents that in the Val-tRNA(Ile) editing reaction. Analyses of the Val-tRNA(Ile) editing activities of T. thermophilus IleRS mutants revealed the importance of Thr(228), Thr(229), Thr(230), and Asp(328), which are coordinated with water molecules in the present structure. The structural model for the Val-adenosine moiety of Val-tRNA(Ile) bound in the IleRS editing site revealed some interesting differences in the substrate binding and recognizing mechanisms between IleRS and T. thermophilus leucyl-tRNA synthetase. For example, the carbonyl oxygens of the amino acids are located opposite to each other, relative to the adenosine ribose ring, and are differently recognized.
About this Structure
1UE0 is a Single protein structure of sequence from Thermus thermophilus. Full crystallographic information is available from OCA.
Reference
Crystal structures of the CP1 domain from Thermus thermophilus isoleucyl-tRNA synthetase and its complex with L-valine., Fukunaga R, Fukai S, Ishitani R, Nureki O, Yokoyama S, J Biol Chem. 2004 Feb 27;279(9):8396-402. Epub 2003 Dec 12. PMID:14672940
Page seeded by OCA on Thu Mar 20 14:30:46 2008
Categories: Isoleucine--tRNA ligase | Single protein | Thermus thermophilus | Fukai, S. | Fukunaga, R. | Ishitani, R. | Nureki, O. | RSGI, RIKEN Structural Genomics/Proteomics Initiative. | Yokoyama, S. | VAL | Aminoacyl-trna synthetase | Cp1 | Editing | National project on protein structural and functional analyse | Nppsfa | Riken structural genomics/proteomics initiative | Rsgi | Structural genomic
