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rdf:type |
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lifeskim:mentions |
umls-concept:C0007382,
umls-concept:C0043393,
umls-concept:C0062773,
umls-concept:C0441712,
umls-concept:C0444626,
umls-concept:C1167622,
umls-concept:C1333931,
umls-concept:C1414639,
umls-concept:C1548174,
umls-concept:C1705535,
umls-concept:C1706076,
umls-concept:C1710236
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pubmed:issue |
5
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pubmed:dateCreated |
2002-1-7
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pubmed:databankReference |
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pubmed:abstractText |
Esa1 is the catalytic subunit of the NuA4 histone acetylase (HAT) complex that acetylates histone H4, and it is a member of the MYST family of HAT proteins that includes the MOZ oncoprotein and the HIV-1 Tat interacting protein Tip60. Here we report the X-ray crystal structure of the HAT domain of Esa1 bound to coenzyme A and investigate the protein's catalytic mechanism. Our data reveal that Esa1 contains a central core domain harboring a putative catalytic base, and flanking domains that are implicated in histone binding. Comparisons with the Gcn5/PCAF and Hat1 proteins suggest a unified mechanism of catalysis and histone binding by HAT proteins, whereby a structurally conserved core domain mediates catalysis, and sequence variability within a structurally related N- and C-terminal scaffold determines substrate specificity.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
1097-2765
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
6
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1195-205
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:11106757-Acetyltransferases,
pubmed-meshheading:11106757-Amino Acid Sequence,
pubmed-meshheading:11106757-Binding Sites,
pubmed-meshheading:11106757-Catalysis,
pubmed-meshheading:11106757-Catalytic Domain,
pubmed-meshheading:11106757-Coenzyme A,
pubmed-meshheading:11106757-Conserved Sequence,
pubmed-meshheading:11106757-Crystallography, X-Ray,
pubmed-meshheading:11106757-Fungal Proteins,
pubmed-meshheading:11106757-Histone Acetyltransferases,
pubmed-meshheading:11106757-Histones,
pubmed-meshheading:11106757-Models, Molecular,
pubmed-meshheading:11106757-Molecular Sequence Data,
pubmed-meshheading:11106757-Mutation,
pubmed-meshheading:11106757-Phenotype,
pubmed-meshheading:11106757-Protein Binding,
pubmed-meshheading:11106757-Protein Structure, Tertiary,
pubmed-meshheading:11106757-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:11106757-Sequence Alignment,
pubmed-meshheading:11106757-Structure-Activity Relationship,
pubmed-meshheading:11106757-Substrate Specificity,
pubmed-meshheading:11106757-Yeasts
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pubmed:year |
2000
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pubmed:articleTitle |
Crystal structure of yeast Esa1 suggests a unified mechanism for catalysis and substrate binding by histone acetyltransferases.
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pubmed:affiliation |
The Wistar Institute University of Pennsylvania, Philadelphia, PA 19104, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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