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Literature summary extracted from

  • Ramakrishnan, B.; Qasba, P.K.
    Crystal structure of the catalytic domain of Drosophila beta1,4-Galactosyltransferase-7 (2010), J. Biol. Chem., 285, 15619-15626.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

EC Number Cloned (Comment) Organism
2.4.1.90 DNA fragments coding the catalytic domain (Cd7) sequence (residues 71-322) and the C-terminal 11-amino acid deletion (Cd7DELTAC) sequence (residues 71-311) are cloned into a pET23a vector and expressed in Escherichia coli Drosophila melanogaster
2.4.1.133 expressed in Escherichia coli Rosetta(DE3)pLysS cells Drosophila melanogaster

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
2.4.1.90 crystal structure of the catalytic domain of beta4Gal-T7 from Drosophila melanogaster in the presence of manganese and UDP at 1.81 A resolution is shown. In the crystal structure, a new manganese ion-binding motif is observed. Superposition of the crystal structures of beta4Gal-T7 and beta4Gal-T1 shows that the catalytic pocket and the substrate-binding sites in these proteins are similar Drosophila melanogaster
2.4.1.133 enzyme in the presence of manganese and UDP, hanging drop vapor diffusion method, using 100 mM Tris-HCl (pH 8.0), 1 M NaCl, 15% (v/v) MPD, and 5% (w/v) polyethylene glycol 6000 Drosophila melanogaster

Protein Variants

EC Number Protein Variants Comment Organism
2.4.1.90 DELTA1-70 crystallization of a refolded Drosophila Cd7 protein coding the catalytic domain (Cd7) sequence (residues 71-322) is not successful Drosophila melanogaster
2.4.1.90 DELTA1-70/DELTA312-322 a DNA fragment bearing the Cd7 catalytic domain and C-terminal 11-amino acid deletion (Cd7DELTAC) sequence (residues 71-311) shows no difference in catalytic activity or folding but crystalization is not possible Drosophila melanogaster
2.4.1.90 additional information a construct bearing the N-terminal peptides from bovine Cd1 (residues 143–175 (P1)) fused with peptide with the Cd7DELTAC protein (last 11 amino acids deleted) shows no impact on the catalytic activity nor the folding efficiency. This construct is used for successful crystallization Drosophila melanogaster

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
2.4.1.133 Mg2+ the Drosophila enzyme exhibits only very low catalytic activity with magnesium Drosophila melanogaster
2.4.1.133 Mn2+ required Drosophila melanogaster

Organism

EC Number Organism UniProt Comment Textmining
2.4.1.90 Drosophila melanogaster
-
-
-
2.4.1.133 Drosophila melanogaster Q8T3P3
-
-

Renatured (Commentary)

EC Number Renatured (Comment) Organism
2.4.1.133 100 mg of sulfonated protein are folded for 48 h in folding solution containing oxido-shuffling agents and 500 mM arginine-HCl Drosophila melanogaster

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.4.1.133 UDP-galactose + O-beta-D-xylosylprotein
-
 Drosophila melanogaster UDP + 4-beta-D-galactosyl-O-beta-D-xylosylprotein
-
 ?

Synonyms

EC Number Synonyms Comment Organism
2.4.1.90 beta1,4-galactosyltransferase-7
-
 Drosophila melanogaster
2.4.1.90 beta4Gal-T7
-
 Drosophila melanogaster
2.4.1.133 beta1,4-galactosyltransferase-7
-
 Drosophila melanogaster
2.4.1.133 beta4Gal-T7
-
 Drosophila melanogaster