Any feedback?
Please rate this page
(all_enzymes.php)
(0/150)

BRENDA support

6.1.1.18: glutamine-tRNA ligase

This is an abbreviated version!
For detailed information about glutamine-tRNA ligase, go to the full flat file.

Word Map on EC 6.1.1.18

Reaction

ATP
+
L-glutamine
+
tRNAGln
=
AMP
+
diphosphate
+
L-glutaminyl-tRNAGln

Synonyms

class I glutaminyl-tRNA synthetase, cytosolic glutaminyl-tRNA synthetase, Gln-RS, Gln4, GlnRS, Glutamine translase, Glutamine--tRNA ligase, Glutamine-tRNA synthetase, glutaminyl tRNA synthetase, Glutaminyl-transfer ribonucleate synthetase, Glutaminyl-transfer RNA synthetase, Glutaminyl-tRNA synthetase, glutaminyltRNA synthetase, glutamyl/glutaminyl-tRNA synthetase, QARS, QRS, Synthetase, glutaminyl-transfer ribonucleate, Vegetative specific protein H4

ECTree

     6 Ligases
         6.1 Forming carbon-oxygen bonds
             6.1.1 Ligases forming aminoacyl-tRNA and related compounds
                6.1.1.18 glutamine-tRNA ligase

Crystallization

Crystallization on EC 6.1.1.18 - glutamine-tRNA ligase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant full-length GlnRS grown in microbatch in the presence of PEG 3350, X-ray diffraction structure determination and analysis at 2.3 A resolution, molecular replacement
vapour-diffusion method. Orthorombic crystals are obtained that belong to space group P2(1)2(1)2(1) and diffract to 2.3 A resolution
-
2.5 A resolution
-
2.8 A resolution
-
analysis of the crystal structure of GlnRS-tRNAGln complex bound to the glutaminyl adenylate analogue 5'-O-[N-(L-Gln)sulfamoyl] adenosine
-
cocrystallization of the purified enzyme with tRNAGln and inhibitor QSI, X-ray diffraction structure determination at 2.4 A resolution and analysis
crystal structure of three misacylating mutants of Escherichia coli glutaminyl-tRNA synthetase complexed with tRNAGln and ATP
-
crystals of the GlnRS-tRNA(2'H)Gln complex bound to the ATP analog AMPCPP and glutamine are grown by microseeding with crystals of the GlnRS-tRNAGln-ATP ternary complex. Crystals grew in 1-2 weeks by vapor diffusion over a reservoir containing 2 M ammonium sulfate, 10 mM Pipes, pH 7.5, 10 mM MgCl2 and 2 mM DTT
-
detailed structural comparison between Met-tRNA synthetase and Gln-tRNA synthetase
-
GlnRS-tRNAGln complex, 6.6 mg/ml protein in 10 mM PIPES, pH 7.5, 10 mM MgCl2, and 1.8-5.4 mM tRNA. The tRNA/analog solution is then mixed with equal volumes of a 6.3 mg/ml solution of GlnRS, containing 5mM PIPES, pH 7.0, and 5 mM 2-mercaptoethanol, X-ray diffraction structure determination and analysis at 2.6 A resolution
purified recombinant GlnRS C229R-tRNAGln complex, a protein solution containing 6.3mg/ml GlnRS prepared in 5 mM PIPES, pH 7.0, 5 mM 2-mercaptoethanol, is mixed with the tRNAGln solution, X-ray diffraction structure determination and analysis at 2.6 A resolution
structure of the enzyme with its cognate glutaminyl-tRNA and ATP
-
the entire anticodon loop provides essential sites for glutaminyl tRNA synthetase discrimination among tRNA molecules
-
purified multisynthetase complex (MSC) subcomplex comprising ArgRS, glutaminyl-tRNA synthetase (GlnRS), and the auxiliary factor aminoacyl tRNA synthetase complex-interacting multifunctional protein 1 (AIMP1)/p43, X-ray diffraction structure determination and analysis
purified recombinant His-tagged wild-type and mutant enzymes, sitting drop vapour diffusion method, apo wild-type GlnRS crystallizes from 0.1 M calcium acetate, 0.1 M Tris, pH 6.0, 12.5% w/v PEG 3350, and 60 mM Gly-Gly-Gly, the Y57H mutant crystallizes from 0.1 M ammonium acetate, 0.1 M Bis-Tris, pH 5.5, and 17% w/v PEG 10 000, and the G45V mutant crystallizes from 0.15 M ammonium acetate, 0.1 M Bis-Tris, pH 5.5, 3% w/v PEG 20 000, and 10 mM EDTA, 16°C, X-ray diffraction strutcure determination and analysis at 2.4 A, 3.3 A, and 2.7 A resolution, respectively
microbatch-under-oil method, using 50 mM NH4Br, 50 mM KC2H3O2, 100 mM HEPES (pH 7.5), and 20% (w/v) polyethylene glycol 20000
purified recombinant His-tagged N-terminal and C-terminal domain fragments, sitting drop vapour diffusion method, mixing of 20 mg/ml protein in 25 mM Tris pH 7.5, 150 mM KCl, and 10 mM MgCl2, with 2 M ammonium sulfate, 5% isopropanol for the N-terminal fragment and 2 M ammonium sulfate for the C-terminal fragment, X-ray diffraction structure determination and analysis. No crystallization conditions can be identified for the full-length protein