2cfo | pdb_00002cfo

NON-DISCRIMINATING GLUTAMYL-TRNA SYNTHETASE FROM THERMOSYNECHOCOCCUS ELONGATUS IN COMPLEX WITH GLU

spinqualitylabelsall models 2cfo, resolution 2.45Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2cfo is a 2 chain structure with sequence from Pcc 6301. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: GLU Activity: Glutamate--tRNA ligase, with EC number 6.1.1.17 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum Function [SYE_THEEB] Non-discriminating glutamyl-tRNA synthetase. Catalyzes the attachment of glutamate to tRNA(Glu) in a two-step reaction: glutamate is first activated by ATP to form Glu-AMP and then transferred to the acceptor end of tRNA(Glu). Acylates both tRNA(Glu) and tRNA(Gln) with glutamate, but has 13-fold higher efficiency with tRNA(Glu). Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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