1pu9: Difference between revisions

From Proteopedia
Jump to navigationJump to search
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,332,843 edits
New page: left|200px<br /><applet load="1pu9" size="450" color="white" frame="true" align="right" spinBox="true" caption="1pu9, resolution 2.3Å" /> '''Crystal Structure of ...
 
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,332,843 edits
No edit summary
 
(15 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:1pu9.gif|left|200px]]<br /><applet load="1pu9" size="450" color="white" frame="true" align="right" spinBox="true"
caption="1pu9, resolution 2.3&Aring;" />
'''Crystal Structure of Tetrahymena GCN5 with Bound Coenzyme A and a 19-residue Histone H3 Peptide'''<br />


==Overview==
==Crystal Structure of Tetrahymena GCN5 with Bound Coenzyme A and a 19-residue Histone H3 Peptide==
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.
<StructureSection load='1pu9' size='340' side='right'caption='[[1pu9]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
<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>
</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>
<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>
<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>
</table>
== 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/pu/1pu9_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=1pu9 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.


==About this Structure==
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>
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].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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]
</div>
[[Category: Protein complex]]
<div class="pdbe-citations 1pu9" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Tetrahymena thermophila]]
[[Category: Tetrahymena thermophila]]
[[Category: Berger, S.L.]]
[[Category: Berger SL]]
[[Category: Clements, A.]]
[[Category: Clements A]]
[[Category: Lo, W.S.]]
[[Category: Lo WS]]
[[Category: Marmorstein, R.]]
[[Category: Marmorstein R]]
[[Category: Pillus, L.]]
[[Category: Pillus L]]
[[Category: Poux, A.N.]]
[[Category: Poux AN]]
[[Category: COA]]
[[Category: coa-binding protein]]
[[Category: gcn5-related n-acetyltransferase]]
[[Category: histone acetyltransferase]]
[[Category: ternary complex]]
 
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 03:00:53 2007''
Retrieved from "https://proteopedia.org/1pu9"