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New page: left|200px<br /><applet load="1qsr" size="450" color="white" frame="true" align="right" spinBox="true" caption="1qsr, resolution 2.0Å" /> '''CRYSTAL STRUCTURE OF ...
 
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[[Image:1qsr.gif|left|200px]]<br /><applet load="1qsr" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1qsr, resolution 2.0&Aring;" />
'''CRYSTAL STRUCTURE OF TETRAHYMENA GCN5 WITH BOUND ACETYL-COENZYME A'''<br />


==Overview==
==CRYSTAL STRUCTURE OF TETRAHYMENA GCN5 WITH BOUND ACETYL-COENZYME A==
Gene activation is a highly regulated process that requires the, coordinated action of proteins to relieve chromatin repression and to, promote transcriptional activation. Nuclear histone acetyltransferase, (HAT) enzymes provide a mechanistic link between chromatin destabilization, and gene activation by acetylating the epsilon-amino group of specific, lysine residues within the aminoterminal tails of core histones to, facilitate access to DNA by transcriptional activators. Here we report the, high-resolution crystal structure of the HAT domain of Tetrahymena GCN5, (tGCN5) bound with both its physiologically relevant ligands, coenzyme A, (CoA) and a histone H3 peptide, and the structures of nascent tGCN5 and a, tGCN5/acetyl-CoA complex. Our structural data reveal histone-binding, specificity for a random-coil structure containing a G-K-X-P recognition, sequence, and show that CoA is essential for reorienting the enzyme for, histone binding. Catalysis appears to involve water-mediated proton, extraction from the substrate lysine by a glutamic acid general base and a, backbone amide that stabilizes the transition-state reaction intermediate., Comparison with related N-acetyltransferases indicates a conserved, structural framework for CoA binding and catalysis, and structural, variability in regions associated with substrate-specific binding.
<StructureSection load='1qsr' size='340' side='right'caption='[[1qsr]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
 
== Structural highlights ==
==About this Structure==
<table><tr><td colspan='2'>[[1qsr]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Tetrahymena_thermophila Tetrahymena thermophila]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QSR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1QSR FirstGlance]. <br>
1QSR is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Tetrahymena_thermophila Tetrahymena thermophila] with ACO as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1QSR OCA].  
</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&#8491;</td></tr>
 
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACO:ACETYL+COENZYME+*A'>ACO</scene></td></tr>
==Reference==
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1qsr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qsr OCA], [https://pdbe.org/1qsr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1qsr RCSB], [https://www.ebi.ac.uk/pdbsum/1qsr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1qsr ProSAT]</span></td></tr>
Structure of Tetrahymena GCN5 bound to coenzyme A and a histone H3 peptide., Rojas JR, Trievel RC, Zhou J, Mo Y, Li X, Berger SL, Allis CD, Marmorstein R, Nature. 1999 Sep 2;401(6748):93-8. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10485713 10485713]
</table>
[[Category: Single protein]]
== 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/qs/1qsr_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=1qsr ConSurf].
<div style="clear:both"></div>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Tetrahymena thermophila]]
[[Category: Tetrahymena thermophila]]
[[Category: Allis, C.David.]]
[[Category: Berger SL]]
[[Category: Berger, S.L.]]
[[Category: David Allis C]]
[[Category: Li, X.]]
[[Category: Li X]]
[[Category: Marmorstein, R.]]
[[Category: Marmorstein R]]
[[Category: Mo, Y.]]
[[Category: Mo Y]]
[[Category: Rojas, J.R.]]
[[Category: Rojas JR]]
[[Category: Trievel, R.C.]]
[[Category: Trievel RC]]
[[Category: Zhou, J.]]
[[Category: Zhou J]]
[[Category: ACO]]
[[Category: coa-binding protein]]
[[Category: gcn5-related n-acetyltransferase]]
[[Category: histone acetyltransferase]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 04:24:16 2007''

Latest revision as of 08:17, 14 February 2024

CRYSTAL STRUCTURE OF TETRAHYMENA GCN5 WITH BOUND ACETYL-COENZYME A

1qsr, resolution 2.00Å

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