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1fy7

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{{STRUCTURE_1fy7| PDB=1fy7 | SCENE= }}
{{STRUCTURE_1fy7| PDB=1fy7 | SCENE= }}
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'''CRYSTAL STRUCTURE OF YEAST ESA1 HISTONE ACETYLTRANSFERASE DOMAIN COMPLEXED WITH COENZYME A'''
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===CRYSTAL STRUCTURE OF YEAST ESA1 HISTONE ACETYLTRANSFERASE DOMAIN COMPLEXED WITH COENZYME A===
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==Overview==
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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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(as it appears on PubMed at http://www.pubmed.gov), where 11106757 is the PubMed ID number.
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{{ABSTRACT_PUBMED_11106757}}
==About this Structure==
==About this Structure==
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[[Category: Coenzyme some]]
[[Category: Coenzyme some]]
[[Category: Histone acetyltransferase]]
[[Category: Histone acetyltransferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 16:54:00 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 04:07:09 2008''

Revision as of 01:07, 1 July 2008

Image:1fy7.png

Template:STRUCTURE 1fy7

CRYSTAL STRUCTURE OF YEAST ESA1 HISTONE ACETYLTRANSFERASE DOMAIN COMPLEXED WITH COENZYME A

Template:ABSTRACT PUBMED 11106757

About this Structure

1FY7 is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

Reference

Crystal structure of yeast Esa1 suggests a unified mechanism for catalysis and substrate binding by histone acetyltransferases., Yan Y, Barlev NA, Haley RH, Berger SL, Marmorstein R, Mol Cell. 2000 Nov;6(5):1195-205. PMID:11106757

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