Molecular cell, 2000-11, Vol.6 (5), p.1195-1205
2000
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Details
- Autor(en) / Beteiligte
- Titel
- Crystal structure of yeast Esa1 suggests a unified mechanism for catalysis and substrate binding by histone acetyltransferases
- Ist Teil von
- Molecular cell, 2000-11, Vol.6 (5), p.1195-1205
- Ort / Verlag
- United States
- Erscheinungsjahr
- 2000
- Quelle
- Elektronische Zeitschriftenbibliothek (Open access)
- Beschreibungen/Notizen
- 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.
- Sprache
- Englisch
- Identifikatoren
- ISSN: 1097-2765eISSN: 1097-4164DOI: 10.1016/S1097-2765(00)00116-7Titel-ID: cdi_proquest_miscellaneous_70513707
- Format
- –
- Schlagworte
- Acetyltransferases - chemistry, Acetyltransferases - classification, Acetyltransferases - genetics, Acetyltransferases - metabolism, Amino Acid Sequence, Binding Sites, Catalysis, Catalytic Domain, Coenzyme A - chemistry, Coenzyme A - metabolism, Conserved Sequence, Crystallography, X-Ray, Esa1 protein, Fungal Proteins - chemistry, Fungal Proteins - classification, Fungal Proteins - genetics, Fungal Proteins - metabolism, Histone Acetyltransferases, Histones - metabolism, Models, Molecular, Molecular Sequence Data, Mutation - genetics, Phenotype, Protein Binding, Protein Structure, Tertiary, Saccharomyces cerevisiae, Saccharomyces cerevisiae Proteins, Sequence Alignment, Structure-Activity Relationship, Substrate Specificity, Yeasts - enzymology, Yeasts - genetics