EC Number   |
|---|
   2.3.1.48 | - |
| 2.3.1.48 | crystal structure of tGcn5 bound to 19-residue histone H4 and P53 peptides |
| 2.3.1.48 | crystallization of the catalytic domains of Gcn5 and p/CAF with a number of peptide substrates including sequences from histone and p53 |
| 2.3.1.48 | in complex with acetyl coenzyme A and histone H4 peptide, i.e. residues 1-20, to 1.9 A resolution. The cofactor and the side chain of lysine 12 of histone H4 peptide are placed in the canyon between the central and C-terminal domains. Histone H4 peptide adopts a well-defined conformation and establishes an extensive set of interactions with the enzyme including invariant residues Glu64 and Trp199, which together govern substrate-binding specificity. There is a cumulative effect of the active-site residues Glu187, Glu276, and Asp277 on deprotonation of the epsilon-amino group of reactive Lys12 for direct attack of the acetyl group of the cofactor |
| 2.3.1.48 | in complex with BRPF2, sitting drop vapor diffusion method, using 2% (w/v) tacsimate (pH 8.0), 0.1 M Tris-HCl (pH 8.5) and 12% (w/v) polyethylene glycol 3350 |
| 2.3.1.48 | modeling of the initial complex between acetyltransferase Gcn5, acetyl-CoA and histone H3 and 20 ns molecular dynamics simulation. Glu80 acts as the general base for deprotonation of residue Lys171 from H3. Glu80, water180 and Lys171 form a proton-wire for the deprotonation process of Lys171. Both loop alpha7-beta7 and loop alpha1-alpha2 play a critical role in binding substrate H3 |
| 2.3.1.48 | molecular model of the complex between enzyme Rtt109 and histone chaperone Vps75 based on X-ray diffraction of crystals. The model reveals distinct negative electrostatic surfaces on an Rtt109 molecule that interface with complementary electropositive ends of a symmetrical Vps75 dimer. Rtt109 variants with interface point substitutions lack the ability to be fully activated by Vps75, yet these variants show no adverse effect on Asf1-dependent Rtt109 activities in vitro and in vivo. Molecular model with a 1:2 complex of Rtt109-Vps75 which acetylates a heterodimer of H3-H4 |
| 2.3.1.48 | purified recombinant detagged enzyme in apoform and bound to acetyl-CoA, hanging drop vapor diffusion method, mixing of 8.5 mg/ml protein solution with reservoir solution contains 16% PEG 1000, 0.2 M calcium acetate, and 0.1 M Tris-HCl, pH 7.0, crystals of acetyl-CoA bound enzyme are obtained by mixing 0.49 mM protein and 0.7 mM acetyl-CoA and equilibrating with a well solution composed of 15% PEG 3350, 0.2 M ammonium citrate dibasic, and 0.1 M Tris-HCl, pH 7.5, 20°C, X-ray diffraction structure determination and analysis at 2.21 A and 1.62 A resolution, respectively, molecular replacement using the putative acetyltransferase YpeA structure (PDB ID 2PDO) as a search model, model building |
| 2.3.1.48 | tGcn5 domain cocrystallized with inhibitor histone H3-methyl-CoA-peptide of 20 amino acid residues, hanging drop vapour diffusion method at 20°C, 2.0 M (NH4)2SO4, 0.1 M Na cacodylate, pH 6.6, 0.2 M NaCl, CoA is bound via isopropionyl linker to Lys14, structure analysis, modeling of conformational changes |
| 2.3.1.48 | the X-ray crystal structures of yeast Esa1 (yEsa1/KAT5) bound to a bisubstrate H4K16CoA inhibitor and human MOF (hMOF/KAT8/MYST1) reveal that they are autoacetylated at a strictly conserved lysine residue in MYST proteins |
