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1fy7

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(New page: 200px<br /><applet load="1fy7" size="450" color="white" frame="true" align="right" spinBox="true" caption="1fy7, resolution 2.0&Aring;" /> '''CRYSTAL STRUCTURE OF ...)
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[[Image:1fy7.gif|left|200px]]<br /><applet load="1fy7" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1fy7.gif|left|200px]]<br /><applet load="1fy7" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1fy7, resolution 2.0&Aring;" />
caption="1fy7, resolution 2.0&Aring;" />
'''CRYSTAL STRUCTURE OF YEAST ESA1 HISTONE ACETYLTRANSFERASE DOMAIN COMPLEXED WITH COENZYME A'''<br />
'''CRYSTAL STRUCTURE OF YEAST ESA1 HISTONE ACETYLTRANSFERASE DOMAIN COMPLEXED WITH COENZYME A'''<br />
==Overview==
==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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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==
==About this Structure==
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1FY7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with NA and COA as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1FY7 OCA].
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1FY7 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with <scene name='pdbligand=NA:'>NA</scene> and <scene name='pdbligand=COA:'>COA</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FY7 OCA].
==Reference==
==Reference==
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[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Barlev, N.A.]]
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[[Category: Barlev, N A.]]
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[[Category: Berger, S.L.]]
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[[Category: Berger, S L.]]
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[[Category: Haley, R.H.]]
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[[Category: Haley, R H.]]
[[Category: Marmorstein, R.]]
[[Category: Marmorstein, R.]]
[[Category: Yan, Y.]]
[[Category: Yan, Y.]]
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[[Category: histone acetyltransferase]]
[[Category: histone acetyltransferase]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 15:27:37 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:43:53 2008''

Revision as of 10:43, 21 February 2008


1fy7, resolution 2.0Å

Drag the structure with the mouse to rotate

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 with and as ligands. 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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