2cfo
From Proteopedia
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'''NON-DISCRIMINATING GLUTAMYL-TRNA SYNTHETASE FROM THERMOSYNECHOCOCCUS ELONGATUS IN COMPLEX WITH GLU''' | '''NON-DISCRIMINATING GLUTAMYL-TRNA SYNTHETASE FROM THERMOSYNECHOCOCCUS ELONGATUS IN COMPLEX WITH GLU''' | ||
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[[Category: Schubert, W D.]] | [[Category: Schubert, W D.]] | ||
[[Category: Schulze, J O.]] | [[Category: Schulze, J O.]] | ||
| - | [[Category: | + | [[Category: Aminoacyl-trna synthetase]] |
| - | [[Category: | + | [[Category: Atp-binding]] |
| - | [[Category: | + | [[Category: Ligase]] |
| - | [[Category: | + | [[Category: Nucleotide-binding]] |
| - | [[Category: | + | [[Category: Protein biosynthesis]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 22:01:29 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 19:01, 3 May 2008
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 Page seeded by OCA on Sat May 3 22:01:29 2008
