1q2c

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[[Image:1q2c.jpg|left|200px]]
 
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{{Structure
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==Crystal Structure of Tetrahymena GCN5 With Bound Coenzyme A and a 19-residue Histone H4 Peptide==
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|PDB= 1q2c |SIZE=350|CAPTION= <scene name='initialview01'>1q2c</scene>, resolution 2.25&Aring;
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<StructureSection load='1q2c' size='340' side='right'caption='[[1q2c]], [[Resolution|resolution]] 2.25&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND= <scene name='pdbligand=COA:COENZYME A'>COA</scene>
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<table><tr><td colspan='2'>[[1q2c]] is a 2 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=1Q2C OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1Q2C FirstGlance]. <br>
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|ACTIVITY=
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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]] 2.25&#8491;</td></tr>
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|GENE=
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<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>
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}}
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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=1q2c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1q2c OCA], [https://pdbe.org/1q2c PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1q2c RCSB], [https://www.ebi.ac.uk/pdbsum/1q2c PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1q2c ProSAT]</span></td></tr>
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</table>
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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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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/q2/1q2c_consurf.spt"</scriptWhenChecked>
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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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</jmolCheckbox>
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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=1q2c ConSurf].
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<div style="clear:both"></div>
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'''Crystal Structure of Tetrahymena GCN5 With Bound Coenzyme A and a 19-residue Histone H4 Peptide'''
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==See Also==
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*[[Histone acetyltransferase 3D structures|Histone acetyltransferase 3D structures]]
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__TOC__
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==Overview==
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</StructureSection>
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Distinct posttranslational modifications on histones occur in specific patterns to mediate certain chromosomal events. For example, on histone H3, phosphorylation at Ser10 can enhance GCN5-mediated Lys14 acetylation to promote transcription. To gain insight into the mechanism underlying this synergism, we determined the structure of Tetrahymena GCN5 (tGCN5) and coenzyme A (CoA) bound to unmodified and Ser10-phosphorylated 19 residue histone H3 peptides (H3p19 and H3p19Pi, respectively). The tGCN5/CoA/H3p19 structure reveals that a 12 amino acid core sequence mediates extensive contacts with the protein, providing the structural basis for substrate specificity by the GCN5/PCAF family of histone acetyltransferases. Comparison with the tGCN5/CoA/H3p19Pi structure reveals that phospho-Ser10 and Thr11 mediate significant histone-protein interactions, and nucleate additional interactions distal to the phosphorylation site. Functional studies show that histone H3 Thr11 is necessary for optimal transcription at yGcn5-dependent promoters requiring Ser10 phosphorylation. Together, these studies reveal how one histone modification can modulate another to affect distinct transcriptional signals.
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[[Category: Large Structures]]
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==About this Structure==
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1Q2C 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=1Q2C OCA].
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==Reference==
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Structural basis for histone and phosphohistone binding by the GCN5 histone acetyltransferase., Clements A, Poux AN, Lo WS, Pillus L, Berger SL, Marmorstein R, Mol Cell. 2003 Aug;12(2):461-73. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14536085 14536085]
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[[Category: Single protein]]
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[[Category: Tetrahymena thermophila]]
[[Category: Tetrahymena thermophila]]
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[[Category: Marmorstein, R.]]
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[[Category: Marmorstein R]]
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[[Category: Poux, A N.]]
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[[Category: Poux AN]]
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[[Category: COA]]
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[[Category: tetrahymena; gcn5; histone h4; x-ray structure]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:32:05 2008''
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Current revision

Crystal Structure of Tetrahymena GCN5 With Bound Coenzyme A and a 19-residue Histone H4 Peptide

PDB ID 1q2c

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