1mjb

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[[Image:1mjb.gif|left|200px]]<br /><applet load="1mjb" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1mjb.gif|left|200px]]
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caption="1mjb, resolution 2.5&Aring;" />
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'''Crystal structure of yeast Esa1 histone acetyltransferase E338Q mutant complexed with acetyl coenzyme A'''<br />
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{{Structure
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|PDB= 1mjb |SIZE=350|CAPTION= <scene name='initialview01'>1mjb</scene>, resolution 2.5&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=ACO:ACETYL COENZYME *A'>ACO</scene>
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|ACTIVITY=
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|GENE= YOR244W ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae])
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}}
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'''Crystal structure of yeast Esa1 histone acetyltransferase E338Q mutant complexed with acetyl coenzyme A'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1MJB 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=ACO:'>ACO</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MJB OCA].
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1MJB 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=1MJB OCA].
==Reference==
==Reference==
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The catalytic mechanism of the ESA1 histone acetyltransferase involves a self-acetylated intermediate., Yan Y, Harper S, Speicher DW, Marmorstein R, Nat Struct Biol. 2002 Nov;9(11):862-9. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12368900 12368900]
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The catalytic mechanism of the ESA1 histone acetyltransferase involves a self-acetylated intermediate., Yan Y, Harper S, Speicher DW, Marmorstein R, Nat Struct Biol. 2002 Nov;9(11):862-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12368900 12368900]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: esa1]]
[[Category: esa1]]
[[Category: hat]]
[[Category: hat]]
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[[Category: histone acetyltransferases]]
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[[Category: histone acetyltransferase]]
[[Category: myst]]
[[Category: myst]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:55:41 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:44:06 2008''

Revision as of 10:44, 20 March 2008


PDB ID 1mjb

Drag the structure with the mouse to rotate
, resolution 2.5Å
Ligands:
Gene: YOR244W (Saccharomyces cerevisiae)
Coordinates: save as pdb, mmCIF, xml



Crystal structure of yeast Esa1 histone acetyltransferase E338Q mutant complexed with acetyl coenzyme A


Overview

Yeast ESA1 is a member of the MYST subfamily of histone acetyltransferases (HATs), which use acetyl-coenzyme A (CoA) to acetylate specific Lys residues within histones to regulate gene expression. The structure of an ESA1-CoA complex reveals structural similarity to the catalytic core of the GCN5/PCAF subfamily of HAT proteins. Here we report additional structural and functional studies on ESA1 that demonstrate that histone acetylation proceeds through an acetyl-cysteine enzyme intermediate. This Cys residue is strictly conserved within the MYST members, suggesting a common mode of catalysis by this HAT subfamily. However, this mode of catalysis differs dramatically from the GCN5/PCAF subfamily, which mediate direct nucleophilic attack of the acetyl-CoA cofactor by the enzyme-deprotonated substrate lysine of the histone. These results demonstrate that different HAT subfamilies can use distinct catalytic mechanisms, which have implications for their distinct biological roles and for the development of HAT-specific inhibitors.

About this Structure

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

Reference

The catalytic mechanism of the ESA1 histone acetyltransferase involves a self-acetylated intermediate., Yan Y, Harper S, Speicher DW, Marmorstein R, Nat Struct Biol. 2002 Nov;9(11):862-9. PMID:12368900

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