1e6i

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{{Seed}}
 
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[[Image:1e6i.png|left|200px]]
 
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==Bromodomain from GCN5 complexed with acetylated H4 peptide==
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The line below this paragraph, containing "STRUCTURE_1e6i", creates the "Structure Box" on the page.
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<StructureSection load='1e6i' size='340' side='right'caption='[[1e6i]], [[Resolution|resolution]] 1.87&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'>[[1e6i]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E6I OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1E6I FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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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]] 1.87&#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=ALY:N(6)-ACETYLLYSINE'>ALY</scene></td></tr>
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{{STRUCTURE_1e6i| PDB=1e6i | 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=1e6i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1e6i OCA], [https://pdbe.org/1e6i PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1e6i RCSB], [https://www.ebi.ac.uk/pdbsum/1e6i PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1e6i ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/GCN5_YEAST GCN5_YEAST] Acetylates histone H2B to form H2BK11ac and H2BK16ac, histone H3 to form H3K9ac, H3K14ac, H3K18ac, H3K23ac, H3K27ac and H3K36ac, with a lower preference histone H4 to form H4K8ac and H4K16ac, and contributes to H2A.Z acetylation. Acetylation of histones gives a specific tag for epigenetic transcription activation. Operates in concert with certain DNA-binding transcriptional activators such as GCN4 or HAP2/3/4. Its acetyltransferase activity seems to be dependent on the association in different multisubunit complexes. Functions as histone acetyltransferase component of the transcription regulatory histone acetylation (HAT) complexes SAGA, SALSA and ADA. SAGA is involved in RNA polymerase II-dependent transcriptional regulation of approximately 10% of yeast genes. At the promoters, SAGA is required for recruitment of the basal transcription machinery. It influences RNA polymerase II transcriptional activity through different activities such as TBP interaction (SPT3, SPT8 and SPT20) and promoter selectivity, interaction with transcription activators (GCN5, ADA2, ADA3 and TRA1), and chromatin modification through histone acetylation (GCN5) and deubiquitination (UBP8). SAGA acetylates nucleosomal histone H3 to some extent (to form H3K9ac, H3K14ac, H3K18ac and H3K23ac). SAGA interacts with DNA via upstream activating sequences (UASs). SALSA, an altered form of SAGA, may be involved in positive transcriptional regulation. The ADA histone acetyltransferase complex preferentially acetylates nucleosomal histones H3 (to form H3K14ac and H3K18ac) and H2B, leading to transcription regulation. SLIK is proposed to have partly overlapping functions with SAGA. It preferentially acetylates methylated histone H3, at least after activation at the GAL1-10 locus.<ref>PMID:10026213</ref> <ref>PMID:16543222</ref> <ref>PMID:16543223</ref>
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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/e6/1e6i_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=1e6i ConSurf].
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<div style="clear:both"></div>
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===BROMODOMAIN FROM GCN5 COMPLEXED WITH ACETYLATED H4 PEPTIDE===
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==See Also==
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*[[Histone acetyltransferase 3D structures|Histone acetyltransferase 3D structures]]
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*[[Transcriptional activator 3D structures|Transcriptional activator 3D structures]]
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== References ==
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The line below this paragraph, {{ABSTRACT_PUBMED_11080160}}, adds the Publication Abstract to the page
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<references/>
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(as it appears on PubMed at http://www.pubmed.gov), where 11080160 is the PubMed ID number.
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__TOC__
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</StructureSection>
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{{ABSTRACT_PUBMED_11080160}}
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[[Category: Large Structures]]
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==About this Structure==
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1E6I is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1E6I OCA].
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==Reference==
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<ref group="xtra">PMID:11080160</ref><references group="xtra"/>
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[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
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[[Category: Evans, P R.]]
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[[Category: Evans PR]]
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[[Category: Owen, D J.]]
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[[Category: Owen DJ]]
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[[Category: Travers, A A.]]
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[[Category: Travers AA]]
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[[Category: Bromodomain]]
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[[Category: Histone binding]]
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[[Category: N-acetyl lysine]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Feb 16 12:12:33 2009''
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Current revision

Bromodomain from GCN5 complexed with acetylated H4 peptide

PDB ID 1e6i

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