1pu9

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(New page: 200px<br /><applet load="1pu9" size="450" color="white" frame="true" align="right" spinBox="true" caption="1pu9, resolution 2.3&Aring;" /> '''Crystal Structure of ...)
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[[Image:1pu9.gif|left|200px]]<br /><applet load="1pu9" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1pu9, resolution 2.3&Aring;" />
 
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'''Crystal Structure of Tetrahymena GCN5 with Bound Coenzyme A and a 19-residue Histone H3 Peptide'''<br />
 
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==Overview==
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==Crystal Structure of Tetrahymena GCN5 with Bound Coenzyme A and a 19-residue Histone H3 Peptide==
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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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<StructureSection load='1pu9' size='340' side='right'caption='[[1pu9]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1pu9]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] and [https://en.wikipedia.org/wiki/Tetrahymena_thermophila Tetrahymena thermophila]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PU9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1PU9 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]] 2.3&#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=COA:COENZYME+A'>COA</scene></td></tr>
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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=1pu9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pu9 OCA], [https://pdbe.org/1pu9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1pu9 RCSB], [https://www.ebi.ac.uk/pdbsum/1pu9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1pu9 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/pu/1pu9_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=1pu9 ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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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==About this Structure==
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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:14536085<ref>PMID:14536085</ref>
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1PU9 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Tetrahymena_thermophila Tetrahymena thermophila] with COA as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1PU9 OCA].
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==Reference==
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=14536085 14536085]
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</div>
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[[Category: Protein complex]]
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<div class="pdbe-citations 1pu9" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
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[[Category: Saccharomyces cerevisiae]]
[[Category: Tetrahymena thermophila]]
[[Category: Tetrahymena thermophila]]
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[[Category: Berger, S.L.]]
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[[Category: Berger SL]]
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[[Category: Clements, A.]]
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[[Category: Clements A]]
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[[Category: Lo, W.S.]]
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[[Category: Lo WS]]
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[[Category: Marmorstein, R.]]
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[[Category: Marmorstein R]]
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[[Category: Pillus, L.]]
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[[Category: Pillus L]]
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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: coa-binding protein]]
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[[Category: gcn5-related n-acetyltransferase]]
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[[Category: histone acetyltransferase]]
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[[Category: ternary complex]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 03:00:53 2007''
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Current revision

Crystal Structure of Tetrahymena GCN5 with Bound Coenzyme A and a 19-residue Histone H3 Peptide

PDB ID 1pu9

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