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References
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[1]
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Resource
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Comments
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X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1-320
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Medline ID
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98394469
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PubMed ID
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9727486
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Journal
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Cell
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Year
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1998
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Volume
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94
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Pages
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427-38
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Authors
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Dutnall RN, Tafrov ST, Sternglanz R, Ramakrishnan V
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Title
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Structure of the histone acetyltransferase Hat1: a paradigm for the GCN5-related N-acetyltransferase superfamily.
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Related PDB
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1bob
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Related UniProtKB
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Q12341
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[2]
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Resource
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Comments
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Medline ID
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PubMed ID
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10384314
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Journal
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Cold Spring Harb Symp Quant Biol
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Year
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1998
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Volume
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63
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Pages
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501-7
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Authors
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Dutnall RN, Tafrov ST, Sternglanz R, Ramakrishnan V
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Title
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Structure of the yeast histone acetyltransferase Hat1: insights into substrate specificity and implications for the Gcn5-related N-acetyltransferase superfamily.
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Related PDB
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Related UniProtKB
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[3]
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Resource
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Comments
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Medline ID
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PubMed ID
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9575221
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Journal
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J Biol Chem
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Year
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1998
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Volume
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273
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Pages
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12599-605
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Authors
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Ruiz-Garcia AB, Sendra R, Galiana M, Pamblanco M, Perez-Ortin JE, Tordera V
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Title
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HAT1 and HAT2 proteins are components of a yeast nuclear histone acetyltransferase enzyme specific for free histone H4.
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Related PDB
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Related UniProtKB
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[4]
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Resource
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Comments
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Medline ID
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PubMed ID
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10393169
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Journal
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EMBO J
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Year
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1999
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Volume
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18
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Pages
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3521-32
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Authors
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Clements A, Rojas JR, Trievel RC, Wang L, Berger SL, Marmorstein R
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Title
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Crystal structure of the histone acetyltransferase domain of the human PCAF transcriptional regulator bound to coenzyme A.
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Related PDB
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Related UniProtKB
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[5]
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Resource
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Comments
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Medline ID
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PubMed ID
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11106757
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Journal
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Mol Cell
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Year
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2000
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Volume
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6
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Pages
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1195-205
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Authors
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Yan Y, Barlev NA, Haley RH, Berger SL, Marmorstein R
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Title
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Crystal structure of yeast Esa1 suggests a unified mechanism for catalysis and substrate binding by histone acetyltransferases.
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Related PDB
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Related UniProtKB
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[6]
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Resource
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Comments
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Medline ID
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PubMed ID
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11437231
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Journal
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Cell Mol Life Sci
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Year
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2001
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Volume
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58
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Pages
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693-703
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Authors
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Marmorstein R
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Title
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Structure and function of histone acetyltransferases.
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Related PDB
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Related UniProtKB
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Comments
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Althought the PDB structure (1bob) binds calcium ion, it is not involved in catalysis. The binding site must be a part of active site, to which histone substrate will be bound.
According to the literature [2] & [4], the catalytic reaction proceeds via a direct nucleophilic attack from the epsilon-amino group of lysine residue of the substrate histone against the carbonyl carbon of the acetate group from acetyl-CoA.
Here, the amino group of the histone lysine must be uncharged for the reaction, although it is normally charged at physiological pH. Thus, a general base must abstract a proton from the amino group to initiate the reaction. According to the papers [4], [5] & [6], Glu255 might act as a general base, to activate the amino group of the lysine from the substrate. Based on its homologous enzyme, the general base, Glu255, must be surrounded by hydrophobic residues that might raise the pKa of the glutamate sidechain and facilitate the proton extraction from the lysine substrate (see [4]).
The activated amino group would make a nucleophilic attack on the carbonyl carbon of acetyl-CoA, forming the tetrahedral intermediate, which can be stabilized by mainchain amide (of, probably, the residue corresponding to Phe220 the enzyme) (see [4]).
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