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[[Image:1mj9.jpg|left|200px]]<br /><applet load="1mj9" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1mj9, resolution 2.50&Aring;" />
'''Crystal structure of yeast Esa1(C304S) mutant complexed with Coenzyme A'''<br />


==Overview==
==Crystal structure of yeast Esa1(C304S) mutant complexed with Coenzyme A==
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.
<StructureSection load='1mj9' size='340' side='right'caption='[[1mj9]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1mj9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MJ9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1MJ9 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=COA:COENZYME+A'>COA</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1mj9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mj9 OCA], [https://pdbe.org/1mj9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1mj9 RCSB], [https://www.ebi.ac.uk/pdbsum/1mj9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1mj9 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/ESA1_YEAST ESA1_YEAST] Catalytic component of the NuA4 histone acetyltransferase (HAT) complex which is involved in epigenetic transcriptional activation of selected genes principally by acetylation of nucleosomal histones H4, H3, H2B, H2A and H2A variant H2A.Z. Acetylates histone H4 to form H4K5ac, H4K8ac, H4K12ac and H4K16ac, histone H3 to form H3K14ac, histone H2B to form H2BK16ac, histone H2A to form H2AK4ac and H2AK7ac, and histone variant H2A.Z to form H2A.ZK14ac. Acetylation of histone H4 is essential for DNA double-strand break repair through homologous recombination. Involved in cell cycle progression. Recruitment to promoters depends on H3K4me.<ref>PMID:9858608</ref> <ref>PMID:10082517</ref> <ref>PMID:10835360</ref> <ref>PMID:10911987</ref> <ref>PMID:12353039</ref> <ref>PMID:15175650</ref> <ref>PMID:15494307</ref> <ref>PMID:15045029</ref> <ref>PMID:15923609</ref>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/mj/1mj9_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1mj9 ConSurf].
<div style="clear:both"></div>


==About this Structure==
==See Also==
1MJ9 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=1MJ9 OCA].
*[[Histone acetyltransferase 3D structures|Histone acetyltransferase 3D structures]]
 
== References ==
==Reference==
<references/>
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]
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Single protein]]
[[Category: Harper S]]
[[Category: Harper, S.]]
[[Category: Marmorstein R]]
[[Category: Marmorstein, R.]]
[[Category: Speicher D]]
[[Category: Speicher, D.]]
[[Category: Yan Y]]
[[Category: Yan, Y.]]
[[Category: COA]]
[[Category: NA]]
[[Category: esa1]]
[[Category: hat]]
[[Category: histone acetyltransferase]]
[[Category: myst]]
 
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Retrieved from "https://proteopedia.org/1mj9"