1qsr: Difference between revisions

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-[[Image:1qsr.gif|left|200px]]
- {{Structure
+==CRYSTAL STRUCTURE OF TETRAHYMENA GCN5 WITH BOUND ACETYL-COENZYME A==
-|PDB= 1qsr |SIZE=350|CAPTION= <scene name='initialview01'>1qsr</scene>, resolution 2.0&Aring;
+<StructureSection load='1qsr' size='340' side='right'caption='[[1qsr]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
-|SITE=
+== Structural highlights ==
-|LIGAND= <scene name='pdbligand=ACO:ACETYL COENZYME *A'>ACO</scene>
+<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>
-|ACTIVITY=
+</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>
-|GENE=
+<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>
-}}
+<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>
+</table>
-'''CRYSTAL STRUCTURE OF TETRAHYMENA GCN5 WITH BOUND ACETYL-COENZYME A'''
+== Function ==
+[https://www.uniprot.org/uniprot/Q27198_TETTH Q27198_TETTH]
+== Evolutionary Conservation ==
-==Overview==
+[[Image:Consurf_key_small.gif|200px|right]]
-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.
+Check<jmol>
+  <jmolCheckbox>
-==About this Structure==
+    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/qs/1qsr_consurf.spt"</scriptWhenChecked>
-QSR 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].
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
+    <text>to colour the structure by Evolutionary Conservation</text>
-==Reference==
+  </jmolCheckbox>
-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]
+</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].
-[[Category: Single protein]]
+<div style="clear:both"></div>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
 [[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://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:42:15 2008''