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5gcn
From Proteopedia
(Difference between revisions)
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| - | [[ | + | ==CATALYTIC DOMAIN OF TETRAHYMENA GCN5 HISTONE ACETYLTRANSFERASE IN COMPLEX WITH COENZYME A== |
| + | <StructureSection load='5gcn' size='340' side='right' caption='[[5gcn]], [[NMR_Ensembles_of_Models | 24 NMR models]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[5gcn]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Tetrahymena_thermophila Tetrahymena thermophila]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5GCN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5GCN FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5gcn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5gcn OCA], [http://www.rcsb.org/pdb/explore.do?structureId=5gcn RCSB], [http://www.ebi.ac.uk/pdbsum/5gcn PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | == 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/gc/5gcn_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/chain_selection.php?pdb_ID=2ata ConSurf]. | ||
| + | <div style="clear:both"></div> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Gene transcription requires the release of inactive DNA from its packaging of histone proteins. Following the discovery of the first transcription-associated histone acetyltransferase, tetrahymena GCN5, it was shown that yeast GCN5 is recruited to the promoter and causes hyper-acetylation of histones and transcriptional activation of target genes, establishing a direct connection between histone acetylation and transcriptional activation. Many other important transcription regulators have been found to have histone acetyltransferase activity, including TAFII230/250, p300/CBP and its associated factor PCAF. Here we present the solution structure of the catalytic domain of tGCN5 (residues 47-210) in complex with coenzyme A. The structure contains two domains; the amino-terminal domain is similar to those of other GCN5-related N-acetyltransferases but the carboxy-terminal domain is not. Coenzyme A binds in a deep hydrophobic pocket between the two domains. Chemical shift changes upon titration with histone H3 peptides indicate a binding site at the domain boundary opposite to the coenzyme A site. The structural data indicate a single-step acetyl-transfer reaction mechanism catalysed by a hydrogen bond to the backbone amide group of leucine 126 and the side-chain carboxyl group of a conserved acidic residue. | ||
| - | + | Solution structure of the catalytic domain of GCN5 histone acetyltransferase bound to coenzyme A.,Lin Y, Fletcher CM, Zhou J, Allis CD, Wagner G Nature. 1999 Jul 1;400(6739):86-9. PMID:10403255<ref>PMID:10403255</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
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==See Also== | ==See Also== | ||
*[[Histone acetyltransferase|Histone acetyltransferase]] | *[[Histone acetyltransferase|Histone acetyltransferase]] | ||
| - | + | == References == | |
| - | == | + | <references/> |
| - | < | + | __TOC__ |
| + | </StructureSection> | ||
[[Category: Tetrahymena thermophila]] | [[Category: Tetrahymena thermophila]] | ||
| - | [[Category: Allis, C D | + | [[Category: Allis, C D]] |
| - | [[Category: Fletcher, C M | + | [[Category: Fletcher, C M]] |
| - | [[Category: Lin, Y | + | [[Category: Lin, Y]] |
| - | [[Category: Wagner, G | + | [[Category: Wagner, G]] |
| - | [[Category: Zhou, J | + | [[Category: Zhou, J]] |
[[Category: Chromatin remodeling]] | [[Category: Chromatin remodeling]] | ||
[[Category: Histone acetyltransferase]] | [[Category: Histone acetyltransferase]] | ||
[[Category: Transcription regulation]] | [[Category: Transcription regulation]] | ||
[[Category: Transferase]] | [[Category: Transferase]] | ||
Revision as of 17:06, 10 December 2014
CATALYTIC DOMAIN OF TETRAHYMENA GCN5 HISTONE ACETYLTRANSFERASE IN COMPLEX WITH COENZYME A
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