1fy7: Difference between revisions
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[[Image:1fy7.gif|left|200px]] | [[Image:1fy7.gif|left|200px]] | ||
'''CRYSTAL STRUCTURE OF YEAST ESA1 HISTONE ACETYLTRANSFERASE DOMAIN COMPLEXED WITH COENZYME A''' | {{Structure | ||
|PDB= 1fy7 |SIZE=350|CAPTION= <scene name='initialview01'>1fy7</scene>, resolution 2.0Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=NA:SODIUM+ION'>NA</scene> and <scene name='pdbligand=COA:COENZYME A'>COA</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''CRYSTAL STRUCTURE OF YEAST ESA1 HISTONE ACETYLTRANSFERASE DOMAIN COMPLEXED WITH COENZYME A''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1FY7 is a [ | 1FY7 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FY7 OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/11106757 11106757] | ||
[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: COA]] | [[Category: COA]] | ||
[[Category: NA]] | [[Category: NA]] | ||
[[Category: coenzyme | [[Category: coenzyme some]] | ||
[[Category: histone acetyltransferase]] | [[Category: histone acetyltransferase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:15:32 2008'' | ||
Revision as of 09:15, 20 March 2008
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| 1fy7, resolution 2.0Å | |||||||||||||
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| Ligands: | NA and COA | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
CRYSTAL STRUCTURE OF YEAST ESA1 HISTONE ACETYLTRANSFERASE DOMAIN COMPLEXED WITH COENZYME A
Overview
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.
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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