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1qsr

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[[Image:1qsr.gif|left|200px]]
 
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==CRYSTAL STRUCTURE OF TETRAHYMENA GCN5 WITH BOUND ACETYL-COENZYME A==
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The line below this paragraph, containing "STRUCTURE_1qsr", creates the "Structure Box" on the page.
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<StructureSection load='1qsr' size='340' side='right'caption='[[1qsr]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<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>
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</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>
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<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>
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{{STRUCTURE_1qsr| PDB=1qsr | SCENE= }}
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<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>
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</table>
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'''CRYSTAL STRUCTURE OF TETRAHYMENA GCN5 WITH BOUND ACETYL-COENZYME A'''
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== Function ==
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[https://www.uniprot.org/uniprot/Q27198_TETTH Q27198_TETTH]
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== Evolutionary Conservation ==
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==Overview==
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[[Image:Consurf_key_small.gif|200px|right]]
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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.
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Check<jmol>
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<jmolCheckbox>
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==About this Structure==
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qs/1qsr_consurf.spt"</scriptWhenChecked>
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1QSR 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=1QSR OCA].
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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==Reference==
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</jmolCheckbox>
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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://www.ncbi.nlm.nih.gov/pubmed/10485713 10485713]
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</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].
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[[Category: Single protein]]
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<div style="clear:both"></div>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Tetrahymena thermophila]]
[[Category: Tetrahymena thermophila]]
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[[Category: Allis, C David.]]
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[[Category: Berger SL]]
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[[Category: Berger, S L.]]
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[[Category: David Allis C]]
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[[Category: Li, X.]]
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[[Category: Li X]]
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[[Category: Marmorstein, R.]]
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[[Category: Marmorstein R]]
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[[Category: Mo, Y.]]
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[[Category: Mo Y]]
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[[Category: Rojas, J R.]]
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[[Category: Rojas JR]]
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[[Category: Trievel, R C.]]
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[[Category: Trievel RC]]
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[[Category: Zhou, J.]]
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[[Category: Zhou J]]
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[[Category: Coa-binding protein]]
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[[Category: Gcn5-related n-acetyltransferase]]
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[[Category: Histone acetyltransferase]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 06:39:54 2008''
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Current revision

CRYSTAL STRUCTURE OF TETRAHYMENA GCN5 WITH BOUND ACETYL-COENZYME A

PDB ID 1qsr

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