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6.1.1.11: serine-tRNA ligase

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

Word Map on EC 6.1.1.11

Reaction

ATP
+
L-serine
 +
tRNASer
=
AMP
 +
diphosphate
 +
L-seryl-tRNASer

Synonyms

62 kDa RNA-binding protein, bacterial SerRS, bacterial type seryl-tRNA synthetase, bacterial-type SerRS, bMbSerRS, methanogenic SerRS, methanogenic type seryl-tRNA synthetase, methanogenic-type SerRS, methanogenic-type SerRSs, methanogenic-type seryl-tRNA synthetase, mMbSerRS, mSerRS, mtSerRS, SARS, SCSerS, Serine transfer RNA synthetase, Serine translase, Serine--tRNA ligase, SerRS, SerRS1, SerRS2, SerRSmt, serS, SERSEC, seryl tRNA synthetase, Seryl-transfer ribonucleate synthetase, Seryl-transfer ribonucleic acid synthetase, Seryl-transfer RNA synthetase, Seryl-tRNA synthetase, seryl-tRNA synthetase 1, seryl-tRNA synthetase 2, seryl-tRNA-synthetase, SerZMo, STS, subclass IIa dimeric SerRS, SvsR, Synthetase, seryl-transfer ribonucleate, tRNASer/seryl-tRNA synthetase, ttSerRS, TT_C0520, VlmL, ZmSerS

ECTree

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

Crystallization

Crystallization on EC 6.1.1.11 - serine-tRNA ligase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure of mtRS in complex with seryl adenylate at 1.65 A resolution, space group P222(1) with unit cell parameters a = 79.9, b = 230 A, c = 135.6 A
recombinant enzyme, hanging drop vapor-diffusion method. Crystals diffract well beyond a resolution of 1.16 A and belong to the orthorhombic space group C222(1), with unit cell parameters a = 79.89, b = 230.42, c = 13560. There is one dimer in the asymmetric unit, with a solvent content of 55%
-
sitting-drop vapour-diffusion method. Crystals grew in a very narrow range of conditions using PEG 8000 as precipitant at room temperature. An appropriate concentration of lithium sulfate was critical for crystal nucleation. Crystals diffracted well beyond a resolution of 1.6 A and were found to belong to the orthorhombic space group C222(1), with unit-cell parameters a = 79.89 A, b = 230.42 A, c = 135.60 A. There is one dimer in the asymmetric unit, with a solvent content of 55%
-
purified isozymes, sitting-drop vapour-diffusion method, 8-14 mg/ml protein in 50 mM Na HEPES, pH 7.6, 150 mM KCl, 10 mM MgCl2, and 8% v/v glycerol, is mixed with reservoir solution containing 100 mM Na MES pH 5.6-5.8, 3.2-3.4 M ammonium sulfate and 0-2% v/v glycerol, equilibration against 0.5 ml of reservoir solution. Binary complexes SerRS-SerSA and SerRS-ATP, SerRS_Ser197 with 15 mM 5'-O-[N-(l-seryl)sulfamoyl]adenosine or 10 mM ATP, are mixed with 100 mM Na MES pH 5.8-6.2, 3.3-3.4 M ammonium sulfate and 0-5% v/v glycerol as precipitant solution, 2-3 days, X-ray diffraction structure determination and analysis at 2.0 A resolution, molecular replacement for analysis of crystal structures of unliganded SerRS and of its complexes with ATP and with a seryl-adenylate analogue
in complex with 5'-O-(N-(L-seryl)-sulfamoyl)adenosine, sitting drop vapor diffusion method, using 20% (w/v) PEG 3350, 0.2 M ammonium fluoride or ammonium formate, and 0.1 M HEPES pH 7.0
mutant enzymes E447K and E156T/R157S, sitting drop vapor diffusion method, using 12% (w/v) PEG 3350, 0.2 M NaCl and 0.1 MTris-HCl (pH 7.5)
purified hsSerRS, sitting-drop vapour diffusion method, 0.01875 ml of protein solution containing 10 mg/ml protein in HCl, pH 7.9, 100 mM NaCl, 10 mM MgCl2, 5% glycerol, 5 mM DTT, with 0.00625 ml of reservoir solution containing 100 mM ammonium sulfate, 22% w/v PEG 3350, 5% glycerol, 200 mM sodium formate pH 7.2, supplemented with 20% v/v glycerol, and equilibration against 0.5 ml of reservoir solution, 12°C, 2 weeks, X-ray diffraction structure determination and analysis at 3.1 A resolution
-
in complex with tRNASec from Aquifex aeolicus, sitting drop vapor diffusion method, using 100 mM trisodium citrate-HCl buffer pH 5.6 containing 2.0 M ammonium sulfate and 200 mM potassium sodium tartrate
-
SerRS free and in complex with ATP, serine and the nonhydrolysable seryl-adenylate analogue 5'-O-(N-serylsulfamoyl) adenosine, X-ray diffraction structure determination and anaylsis at 2.5 A resolution
-
crystal structures of the SerRS from the archaeon Pyrococcus horikoshii bound with 5'-O-[N-(L-seryl)-sulfamoyl]-adenosine are solved at 2.6 A, with ATP at 2.8 A, and in the apo form at 3.0 A. SerRS recognizes the seryl and adenylate moieties in a manner similar to those of the bacterial and mitochondrial SerRSs from Thermus thermophilus and Bos taurus, respectively, but different from that of the unusual SerRS from the methanogenic archaeon Methanosarcina barkeri
crystal structure analysis for identification of the amino acid substrate discrimination mechanism
enzyme complexes: 1. with seryl-AMP, 2. with 5'-O-[N-(L-seryl)-sulfamoyl]adenosine
-
structure at 2.3-2.6 A resolution, of enzyme complexes: 1. with ATP and Mn2+, 2. containing seryl-adenylate in the active site, 3. between the enzyme, Ap4A and Mn2+
-
tRNASer-seryl-tRNA synthetase complex, X-ray diffraction structure determination and analysis at 2.9 A resolution, the 1.8 A-resolution tRNASer acceptor stem crystal structure is superimposed to a 2.9 A-resolution crystal structure of a tRNASer-seryl-tRNA synthetase complex for a visualization of the binding environment of the tRNASer microhelix, modeling