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6.1.1.23: aspartate-tRNAAsn ligase

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

Word Map on EC 6.1.1.23

Reaction

ATP
+
L-aspartate
+
tRNAAsx
=
AMP
+
diphosphate
+
L-aspartyl-tRNAAsx

Synonyms

aspartate tRNA synthetase, Aspartic acid translase, Aspartyl ribonucleic synthetase, aspartyl tRNA synthetase, aspartyl-transfer ribonucleate synthetase, Aspartyl-transfer ribonucleic acid synthetase, Aspartyl-transfer RNA synthetase, Aspartyl-tRNA synthetase, AspRS, EC 6.1.1.12, More, ND-AspRS, non-discriminating aspartyl-tRNA synthetase, nondicriminating AspRS, nondiscriminating aspartyl-tRNA synthetase, nondiscriminating AspRS, Synthetase, aspartyl-transfer ribonucleate

ECTree

     6 Ligases
         6.1 Forming carbon-oxygen bonds
             6.1.1 Ligases forming aminoacyl-tRNA and related compounds
                6.1.1.23 aspartate-tRNAAsn ligase

Crystallization

Crystallization on EC 6.1.1.23 - aspartate-tRNAAsn ligase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified AspRS, sitting drop vapour diffusion method, 0.0002 ml of 9 mg/ml protein is mixed with 0.0002 ml of reservoir solution containing 0.2 M lithium sulfate, 0.1 M Bis-Tris, pH 5.5, and 23% w/v PEG 3350, X-ray diffraction structure determination and analysis at 2.8 A resolution
N-terminal anticodon-binding domain of non-discriminating aspartyl-tRNA synthetase, hanging drop vapor diffusion method, using 30% (w/v) PEG 4000, 100 mM ammonium sulfate, 100 mM sodium citrate at pH 5.6
-
purified recombinant enzyme, 5-8 mg/ml in 20 mM Tris–HCl buffer, pH 7.0, hanging-drop vapour-diffusion method, 26°C, from 0.002 ml protein solution is mixed with 0.002 ml of reservoir solution containing 100 mM sodium HEPES buffer, pH 7.5, containing 100 mM NaCl and 1.6 M (NH4)2SO4, equilibration against 0.7 ml reservoir solution, X-ray diffraction structure determination and analysis at 2.3 A resolution, molecular replacement
-
purified recombinant enzyme, X-ray diffraction structure determination and analysis at 2.3 A resolution
-
hanging drop technique, 24°C, 5 days in Crystal Screen I or II, solutions containing either polyethylene glycol or ethylene glycol
-
a complete dataset of the transamidosome is collected to 3 A resolution
-
purified 520 kDa transamidosome complex formed by two dimeric nondiscriminating-AspRSs, two trimeric GatCABs, and four tRNAsAsn molecules, X-ray diffraction structure determination and analysis at 3.0 A resolution, molecular replacement
-