Abstract
We have solved the crystal structure of the yeast histone acetyltransferase Hat1-acetyl coenzyme A (AcCoA) complex at 2.3 A resolution. Hat1 has an elongated, curved structure, and the AcCoA molecule is bound in a cleft on the concave surface of the protein, marking the active site of the enzyme. A channel of variable width and depth that runs across the protein is probably the binding site for the histone substrate. A model for histone H4 binding by Hat1 is discussed in terms of possible sources of specific lysine recognition by the enzyme. The structure of Hat1 provides a model for the structures of the catalytic domains of a protein superfamily that includes other histone acetyltransferases such as Gcn5 and CBP.
Publication types
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Comparative Study
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, Non-P.H.S.
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Research Support, U.S. Gov't, P.H.S.
MeSH terms
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Acetyl Coenzyme A / chemistry*
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Acetyltransferases / chemistry*
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Acetyltransferases / genetics
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Acetyltransferases / metabolism
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Amino Acid Sequence
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Arylamine N-Acetyltransferase / chemistry
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Binding Sites
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Catalysis
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Crystallography
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DNA-Binding Proteins*
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Fungal Proteins / chemistry
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Histone Acetyltransferases
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Histones / metabolism
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Models, Molecular
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Molecular Sequence Data
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Multigene Family
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Protein Conformation
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Protein Kinases / chemistry
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Protein Structure, Secondary
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Recombinant Proteins / chemistry
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Saccharomyces cerevisiae / enzymology
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Saccharomyces cerevisiae Proteins*
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Sequence Homology, Amino Acid
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Synchrotrons
Substances
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DNA-Binding Proteins
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Fungal Proteins
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Histones
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Recombinant Proteins
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Saccharomyces cerevisiae Proteins
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Acetyl Coenzyme A
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Acetyltransferases
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GCN5 protein, S cerevisiae
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Histone Acetyltransferases
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histone acetyltransferase type B complex
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Arylamine N-Acetyltransferase
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Protein Kinases