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[[Image:5gcn.gif|left|200px]]
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{{STRUCTURE_5gcn|  PDB=5gcn  |  SCENE=  }}
'''CATALYTIC DOMAIN OF TETRAHYMENA GCN5 HISTONE ACETYLTRANSFERASE IN COMPLEX WITH COENZYME A'''


==CATALYTIC DOMAIN OF TETRAHYMENA GCN5 HISTONE ACETYLTRANSFERASE IN COMPLEX WITH COENZYME A==
<StructureSection load='5gcn' size='340' side='right'caption='[[5gcn]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5gcn]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Tetrahymena_thermophila Tetrahymena thermophila]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5GCN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5GCN FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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></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=5gcn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5gcn OCA], [https://pdbe.org/5gcn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5gcn RCSB], [https://www.ebi.ac.uk/pdbsum/5gcn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5gcn ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/Q27198_TETTH Q27198_TETTH]
== 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/gc/5gcn_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=5gcn ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Gene transcription requires the release of inactive DNA from its packaging of histone proteins. Following the discovery of the first transcription-associated histone acetyltransferase, tetrahymena GCN5, it was shown that yeast GCN5 is recruited to the promoter and causes hyper-acetylation of histones and transcriptional activation of target genes, establishing a direct connection between histone acetylation and transcriptional activation. Many other important transcription regulators have been found to have histone acetyltransferase activity, including TAFII230/250, p300/CBP and its associated factor PCAF. Here we present the solution structure of the catalytic domain of tGCN5 (residues 47-210) in complex with coenzyme A. The structure contains two domains; the amino-terminal domain is similar to those of other GCN5-related N-acetyltransferases but the carboxy-terminal domain is not. Coenzyme A binds in a deep hydrophobic pocket between the two domains. Chemical shift changes upon titration with histone H3 peptides indicate a binding site at the domain boundary opposite to the coenzyme A site. The structural data indicate a single-step acetyl-transfer reaction mechanism catalysed by a hydrogen bond to the backbone amide group of leucine 126 and the side-chain carboxyl group of a conserved acidic residue.


==Overview==
Solution structure of the catalytic domain of GCN5 histone acetyltransferase bound to coenzyme A.,Lin Y, Fletcher CM, Zhou J, Allis CD, Wagner G Nature. 1999 Jul 1;400(6739):86-9. PMID:10403255<ref>PMID:10403255</ref>
Gene transcription requires the release of inactive DNA from its packaging of histone proteins. Following the discovery of the first transcription-associated histone acetyltransferase, tetrahymena GCN5, it was shown that yeast GCN5 is recruited to the promoter and causes hyper-acetylation of histones and transcriptional activation of target genes, establishing a direct connection between histone acetylation and transcriptional activation. Many other important transcription regulators have been found to have histone acetyltransferase activity, including TAFII230/250, p300/CBP and its associated factor PCAF. Here we present the solution structure of the catalytic domain of tGCN5 (residues 47-210) in complex with coenzyme A. The structure contains two domains; the amino-terminal domain is similar to those of other GCN5-related N-acetyltransferases but the carboxy-terminal domain is not. Coenzyme A binds in a deep hydrophobic pocket between the two domains. Chemical shift changes upon titration with histone H3 peptides indicate a binding site at the domain boundary opposite to the coenzyme A site. The structural data indicate a single-step acetyl-transfer reaction mechanism catalysed by a hydrogen bond to the backbone amide group of leucine 126 and the side-chain carboxyl group of a conserved acidic residue.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
5GCN is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Tetrahymena_thermophila Tetrahymena thermophila]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5GCN OCA].
</div>
<div class="pdbe-citations 5gcn" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
Solution structure of the catalytic domain of GCN5 histone acetyltransferase bound to coenzyme A., Lin Y, Fletcher CM, Zhou J, Allis CD, Wagner G, Nature. 1999 Jul 1;400(6739):86-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10403255 10403255]
*[[Histone acetyltransferase 3D structures|Histone acetyltransferase 3D structures]]
[[Category: Single protein]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Tetrahymena thermophila]]
[[Category: Tetrahymena thermophila]]
[[Category: Allis, C D.]]
[[Category: Allis CD]]
[[Category: Fletcher, C M.]]
[[Category: Fletcher CM]]
[[Category: Lin, Y.]]
[[Category: Lin Y]]
[[Category: Wagner, G.]]
[[Category: Wagner G]]
[[Category: Zhou, J.]]
[[Category: Zhou J]]
[[Category: Chromatin remodeling]]
[[Category: Histone acetyltransferase]]
[[Category: Transcription regulation]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 22:34:36 2008''
Retrieved from "https://proteopedia.org/5gcn"