1fy7
From Proteopedia
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|PDB= 1fy7 |SIZE=350|CAPTION= <scene name='initialview01'>1fy7</scene>, resolution 2.0Å | |PDB= 1fy7 |SIZE=350|CAPTION= <scene name='initialview01'>1fy7</scene>, resolution 2.0Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1fy7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fy7 OCA], [http://www.ebi.ac.uk/pdbsum/1fy7 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1fy7 RCSB]</span> | ||
}} | }} | ||
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[[Category: Marmorstein, R.]] | [[Category: Marmorstein, R.]] | ||
[[Category: Yan, Y.]] | [[Category: Yan, Y.]] | ||
| - | [[Category: COA]] | ||
| - | [[Category: NA]] | ||
[[Category: coenzyme some]] | [[Category: coenzyme some]] | ||
[[Category: histone acetyltransferase]] | [[Category: histone acetyltransferase]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:32:36 2008'' |
Revision as of 17:32, 30 March 2008
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| , resolution 2.0Å | |||||||
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| Ligands: | , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| 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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