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2.3.1.31: homoserine O-acetyltransferase

This is an abbreviated version!
For detailed information about homoserine O-acetyltransferase, go to the full flat file.

Word Map on EC 2.3.1.31

Reaction

acetyl-CoA
+
L-homoserine
=
CoA
 +
O-acetyl-L-homoserine

Synonyms

acetyltransferase, homoserine, CnHTA, DcsE, HAT, homoserine acetyltransferase, homoserine O-acetyltransferase, homoserine transacetylase, homoserine transsuccinylase, homoserine-O-transacetylase, HTA, HTS, L-homoserine O-acetyltransferase, MaHTA, MaMetX, MET2, MetA, MetX, MetXA, metX_1, metX_2, MhHTA, MhMetX, MsHAT, MtHTA, MtMetX, TmHTS

ECTree

     2 Transferases
         2.3 Acyltransferases
             2.3.1 Transferring groups other than aminoacyl groups
                2.3.1.31 homoserine O-acetyltransferase

Crystallization

Crystallization on EC 2.3.1.31 - homoserine O-acetyltransferase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
enzyme in complex with homoserine, hanging drop vapor diffusion, purified protein is added to 1.4 M (NH4)2SO4 and 0.1 M Tris, pH 8.0, soaked with 1.8 M (NH4)2SO4 and same buffer containing 15% glycerol, and 10 mM homoserine, crystals are flash frozen
-
x-ray crystal structure at 2.0 A of the Bacillus cereus metA protein in complex with homoserine is presented
-
hanging drop vapor diffusion method, crystal structure to a resolution of 1.65 A. The structure identifies this enzyme to be a member of the alpha/beta-hydrolase superfamily, possessing an additional lid domain with a novel fold
crystal structure of HTA from Leptospira interrogans is determined at 2.2 A resolution using selenomethionyl single-wavelength anomalous diffraction method. HTA is modular and consists of two structurally distinct domains: a core alpha/beta domain containing the catalytic site and a helical bundle called the lid domain. Structure fold belongs to alpha/beta hydrolase superfamily with the characteristic catalytic triad residues in the active site. The catalytic His and Ser are both present in two conformations, which may be involved in the catalytic mechanism for acetyl transfer
purified enzyme, vapor diffusion hanging drop method, mixing of 0.001 ml of 13.8 mg/ml protein solution with 0.001 ml of well solution containing 0.1 M Tris-HCl, pH 8.5, and 1.8 M magnesium sulfate, 18°C, several days, X-ray diffraction structure determination and analysis at 1.90-1.95 A resolution, molecular replacement using the MaMetX structure as a search model
purified enzyme, vapor diffusion hanging drop method, mixing of 0.001 ml of 13.8 mg/ml protein solution with 0.001 ml of well solution 1.2 M NaH2PO4, 0.8 M K2HPO4, 0.2 M Li sulphate, and 0.1 M CHES, pH 9.0, 18°C, several days, X-ray diffraction structure determination and analysis at 1.69-1.73 A resolution, molecular replacement using the MhMetX structure as a search model
purified enzyme, vapor diffusion hanging drop method, mixing of 0.001 ml of 13.8 mg/ml protein solution with 0.001 ml of well solution containing 0.2 M Ca acetate, and 20% PEG 3350, 18°C, several days, X-ray diffraction structure determination and analysis at 1.47-1.51 A resolution, molecular replacement using the structure of homoserine O-acetyltransferase from Bacillus anthracis (PDB ID 3I1I) as a search model
purified recombinant His-tagged enzyme in apo-form and in complex with either CoA or homoserine, hanging drop vapor diffusion method, mixing of 0.001 ml of protein solution containing 40 mg/ml protein, and 40 mM Tris-HCl, pH 8.0, with 0.001 ml of reservoir solution containing 34% w/v PEG 400, 0.1 M sodium acetate/acetic acid, pH 5.5, and 0.2 M calcium acetate hydrate, and additionally 10 mM ligand for the complex crystals, equilibrating against 0.5 ml of reservoir solution, 20°C, X-ray diffraction structure determination and analysis at 1.55 A resolution
purified recombinant apoenzyme, hanging-drop vapor-diffusion method, mixing of 0.001 ml of 5 mg/ml protein solution with 0.001 ml of well solution, containing 0.7 M ammonium formate, 100 mM imidazole-HCl, pH 6.5, 20°C, 5-7 days, X-ray diffraction structure determination and analysis at 2.45 A resolution
-
purified recombinant wild-type and mutant G52A-P55G enzymes, sitting drop vapor diffusion method, mixing of 0.001 ml of 10 mg/ml of protein in 20 mM Tris-HCl, pH 7.6, 0.2 M NaCl, 5 mM dithiothreitol, and 1 mM EDTA, with 0.001 ml of precipitant solution containing 0.1 M Tris-HCl, pH 7.5, 25% w/v PEG 4000, and 0.2 M ammonium acetate, 3 weeks, structure modeling, X-ray diffraction structure determination and analysis at 1.7-1.8 A resolution