2cfo
From Proteopedia
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| - | [[Image:2cfo.gif|left|200px]] | + | [[Image:2cfo.gif|left|200px]] |
| - | + | ||
| - | '''NON-DISCRIMINATING GLUTAMYL-TRNA SYNTHETASE FROM THERMOSYNECHOCOCCUS ELONGATUS IN COMPLEX WITH GLU''' | + | {{Structure |
| + | |PDB= 2cfo |SIZE=350|CAPTION= <scene name='initialview01'>2cfo</scene>, resolution 2.45Å | ||
| + | |SITE= <scene name='pdbsite=AC1:GLU+Binding+Site+For+Chain+A'>AC1</scene> | ||
| + | |LIGAND= <scene name='pdbligand=GLU:GLUTAMIC ACID'>GLU</scene> | ||
| + | |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= | ||
| + | }} | ||
| + | |||
| + | '''NON-DISCRIMINATING GLUTAMYL-TRNA SYNTHETASE FROM THERMOSYNECHOCOCCUS ELONGATUS IN COMPLEX WITH GLU''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2CFO is a [ | + | 2CFO is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Synechococcus_elongatus Synechococcus elongatus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CFO OCA]. |
==Reference== | ==Reference== | ||
| - | Crystal structure of a non-discriminating glutamyl-tRNA synthetase., Schulze JO, Masoumi A, Nickel D, Jahn M, Jahn D, Schubert WD, Heinz DW, J Mol Biol. 2006 Sep 1;361(5):888-97. Epub 2006 Jul 5. PMID:[http:// | + | Crystal structure of a non-discriminating glutamyl-tRNA synthetase., Schulze JO, Masoumi A, Nickel D, Jahn M, Jahn D, Schubert WD, Heinz DW, J Mol Biol. 2006 Sep 1;361(5):888-97. Epub 2006 Jul 5. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16876193 16876193] |
[[Category: Glutamate--tRNA ligase]] | [[Category: Glutamate--tRNA ligase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: protein biosynthesis]] | [[Category: protein biosynthesis]] | ||
| - | ''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 16:14:48 2008'' |
Revision as of 14:14, 20 March 2008
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| , resolution 2.45Å | |||||||
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| Sites: | |||||||
| Ligands: | |||||||
| Activity: | Glutamate--tRNA ligase, with EC number 6.1.1.17 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
NON-DISCRIMINATING GLUTAMYL-TRNA SYNTHETASE FROM THERMOSYNECHOCOCCUS ELONGATUS IN COMPLEX WITH GLU
Overview
Error-free protein biosynthesis is dependent on the reliable charging of each tRNA with its cognate amino acid. Many bacteria, however, lack a glutaminyl-tRNA synthetase. In these organisms, tRNA(Gln) is initially mischarged with glutamate by a non-discriminating glutamyl-tRNA synthetase (ND-GluRS). This enzyme thus charges both tRNA(Glu) and tRNA(Gln) with glutamate. Discriminating GluRS (D-GluRS), found in some bacteria and all eukaryotes, exclusively generates Glu-tRNA(Glu). Here we present the first crystal structure of a non-discriminating GluRS from Thermosynechococcus elongatus (ND-GluRS(Tel)) in complex with glutamate at a resolution of 2.45 A. Structurally, the enzyme shares the overall architecture of the discriminating GluRS from Thermus thermophilus (D-GluRS(Tth)). We confirm experimentally that GluRS(Tel) is non-discriminating and present kinetic parameters for synthesis of Glu-tRNA(Glu) and of Glu-tRNA(Gln). Anticodons of tRNA(Glu) (34C/UUC36) and tRNA(Gln) (34C/UUG36) differ only in base 36. The pyrimidine base of C36 is specifically recognized in D-GluRS(Tth) by the residue Arg358. In ND-GluRS(Tel) this arginine residue is replaced by glycine (Gly366) presumably allowing both cytosine and the bulkier purine base G36 of tRNA(Gln) to be tolerated. Most other ND-GluRS share this structural feature, leading to relaxed substrate specificity.
About this Structure
2CFO is a Single protein structure of sequence from Synechococcus elongatus. Full crystallographic information is available from OCA.
Reference
Crystal structure of a non-discriminating glutamyl-tRNA synthetase., Schulze JO, Masoumi A, Nickel D, Jahn M, Jahn D, Schubert WD, Heinz DW, J Mol Biol. 2006 Sep 1;361(5):888-97. Epub 2006 Jul 5. PMID:16876193
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