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2.3.1.48: histone acetyltransferase

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

Word Map on EC 2.3.1.48

Reaction

acetyl-CoA
+
[protein]-L-lysine
=
CoA
 +
[protein]-N6-acetyl-L-lysine

Synonyms

AAPatA, acetyltransferase, histone, Ada2/Ada3/Gcn5 complex, AIB1, amino acid sensing acetyltransferase, AmiPatA, Amir 5672, ARD1, ARD1 acetyltransferase, arginine methyltransferase A, arginine methyltransferase B, arrest defective 1, arrest defective protein 1 acetyltransferase, At3g14980, ATAC2, ATase1, ATase2, cAMP-regulated protein lysine acetyltransferase, Cbp, CBP histone acetyltransferase, CBP/p300, chameau, circadian locomoter output cycles protein kaput, CLOCK, CREB binding protein, CREB-binding protein, CREBBP, east1, ELO3, ELONGATA3, elongator protein 3, ELP3, enhancer-of-asymmetric leaves-two1, Enok, EP300, Esa1, factor acetyltransferase, FAT, Gcn5, GCN5 family KAT, Gcn5 HAT, GCN5 lysine acetyltransferase, GCN5 N acetyltransferase 5, Gcn5 related N-acetyltransferase, GCN5-like acetyltransferase, GCN5-like enzyme, GCN5-related N-acetyltransferase, Gcn5/PCAF histone acetyltransferase, GCN5b, GCN5L2, general control non-derepressible 5, general control non-repressed protein5, general control nonderepressible 5, general control nonrepressed-protein 5, general control of amino acid synthesis 5, GNAT, GNAT-related histone acetyltransferase complex, GTF3C4, H4 lysine acetyltransferase, HAC1, HAG1, HAG3, HAG4, HAG5, HAM1, HAM2, hARD1, HAT, HAT-B, HAT-B complex, Hat1, Hat1p, Hat2, HatB3.I, HBO1, histone (H4 K16) acetyltransferase, histone acetokinase, histone acetyl transferase, histone acetylase, histone acetyltransferase, histone acetyltransferase 1, histone acetyltransferase AtGCN5, histone acetyltransferase B, histone acetyltransferase Tip60, histone acetyltransferase-1, histone acetyltransferases, histone H3 acetyltransferase, histone H4 acetyltransferase, histone H4 lysine 16 acetyltransferase, histone transacetylase, histone/protein lysine acetyltransferase, HIV-1 Tat-interactive protein, hMOF, Hpa2, Hpa3, human acetylase binding to ORC1, Idm1, K (lysine) acetyltransferase 8, K(lysine) acetyltransferase 8, KAT, KAT10, KAT11, KAT12, KAT13A, KAT13B, KAT13C, KAT13D, KAT2, Kat2A, KAT2A/GCN5, Kat2b, KAT3A, KAT3B, KAT4, KAT5, KAT6, KAT6A, KAT6B, KAT7, KAT8, KAT9, Lsy-12, lysine acetyltransferase, lysine acetyltransferase 2, lysine acetyltransferase 2A, lysine acetyltransferase 2B, lysine acetyltransferase 5, lysine acetyltransferase 8, lysine acetyltransferase complex, lysine acetyltransferase p300, lysine acetyltransferases, lysine-acetyltransferase, Mof, monocytic leukemia zinc finger, monocytic leukemia zinc finger protein, More, Morf, MORF histone acetyltransferase, MOZ, MOZ histone acetyltransferase, Moz related factor, Mst1, MtPat, Myb-binding protein 1A, MYBBP1A, MYST, MYST protein lysine acetyltransferase, MYST-related histone acetyltransferase complex, MYST1, MYST2, MYST3, MYST4, N(alpha)-acetyltransferase 10, N-acetyltransferase, N-terminal acetyltransferase, NAA10, NAT, NAT4, NCoA-1, NCoA-3, NCOAT, Nepsilon-lysine acetyltransferase, NuA4, NuA4 histone acetyltransferase, nuclear cytoplasmicO-GlcNAcase and acetyltransferase, nuclear receptor coactivator 1, nuclear receptor coactivator 3, nucleosome-histone acetyltransferase, Nut1, p/CAF, P/CAF histone acetyltransferase, p160, p300, p300 HAT, p300 histone acetyltransferase, p300/CBP, p300/CBP associated factor, p300/CBP histone acetyltransferase, P300/CBP-associated factor, p300/CBP-associated factor (pCAF), p300HAT, PA4534, Pat, PCAF, PCAF histone acetyltransferase, PF11_0192, PfGCN5, PfGCN5 HAT, Piccolo NuA4 complex, protein acetyl-transferase, protein acetyltransferase, Qkf, regulator of Ty1 transposition protein 109, RmtA, RmtB, RPD3, Rtt109, Rv0998, SAS complex, Sas2, Sas3, SRC1, SRC3, Sven 0867, SvePatA, TAF, TAF1, Tat interacting protein of 60 kDa, Tat-interactive protein, 60 kDa, TBP1, TFIIIC90, tGCN5, TgGCN5b, TgMYST-B, Tip60, tumor suppressor histone H3 lysine 23 acetyltransferase, type B histone acetyltransferase, YfmK, zMoz

ECTree

     2 Transferases
         2.3 Acyltransferases
             2.3.1 Transferring groups other than aminoacyl groups
                2.3.1.48 histone acetyltransferase

Crystallization

Crystallization on EC 2.3.1.48 - histone acetyltransferase

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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
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
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
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
-
visualization of multifunctional transcription activator p300 by atomic force microscopy. p300 is almost prolate ellipsoidal in shape, having several bulges. The functionally significant N-terminal and C-terminal regions are located near one end and centre of the molecule, respectively. The presence of N- and C-terminal regions near the central portion of the prolate ellipsoid suggests that all four domain could exist spatially close near the central portion of the molecule and hence capable of binding all four domains simultaneously. The complex between p300 and tumor suppressor protein p53 is elongated in shape. p53 binds at the central region of p300
-
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
crystallization of the catalytic domains of Gcn5 and p/CAF with a number of peptide substrates including sequences from histone and p53
-
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
-
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
crystal structure of tGcn5 bound to 19-residue histone H4 and P53 peptides
-
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
-