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1cm0

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(New page: 200px<br /> <applet load="1cm0" size="450" color="white" frame="true" align="right" spinBox="true" caption="1cm0, resolution 2.3&Aring;" /> '''CRYSTAL STRUCTURE OF...)
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[[Image:1cm0.gif|left|200px]]<br />
 
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<applet load="1cm0" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1cm0, resolution 2.3&Aring;" />
 
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'''CRYSTAL STRUCTURE OF THE PCAF/COENZYME-A COMPLEX'''<br />
 
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==Overview==
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==CRYSTAL STRUCTURE OF THE PCAF/COENZYME-A COMPLEX==
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The human p300/CBP-associating factor, PCAF, mediates transcriptional, activation through its ability to acetylate nucleosomal histone substrates, as well as transcriptional activators such as p53. We have determined the, 2.3 A crystal structure of the histone acetyltransferase (HAT) domain of, PCAF bound to coenzyme A. The structure reveals a central protein core, associated with coenzyme A binding and a pronounced cleft that sits over, the protein core and is flanked on opposite sides by the N- and C-terminal, protein segments. A correlation of the structure with the extensive, mutagenesis data for PCAF and the homologous yeast GCN5 protein implicates, the cleft and the N- and C-terminal protein segments as playing an, important role in histone substrate binding, and a glutamate residue in, the protein core as playing an essential catalytic role. A structural, comparison with the coenzyme-bound forms of the related, N-acetyltransferases, HAT1 (yeast histone acetyltransferase 1) and SmAAT, (Serratia marcescens aminoglycoside 3-N-acetyltransferase), suggests the, mode of substrate binding and catalysis by these enzymes and establishes a, paradigm for understanding the structure-function relationships of other, enzymes that acetylate histones and transcriptional regulators to promote, activated transcription.
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<StructureSection load='1cm0' size='340' side='right'caption='[[1cm0]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
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== Structural highlights ==
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==About this Structure==
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<table><tr><td colspan='2'>[[1cm0]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CM0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CM0 FirstGlance]. <br>
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1CM0 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] 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=1CM0 OCA].
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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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==Reference==
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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=1cm0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cm0 OCA], [https://pdbe.org/1cm0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cm0 RCSB], [https://www.ebi.ac.uk/pdbsum/1cm0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cm0 ProSAT]</span></td></tr>
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Crystal structure of the histone acetyltransferase domain of the human PCAF transcriptional regulator bound to coenzyme A., Clements A, Rojas JR, Trievel RC, Wang L, Berger SL, Marmorstein R, EMBO J. 1999 Jul 1;18(13):3521-32. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=10393169 10393169]
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/KAT2B_HUMAN KAT2B_HUMAN] Functions as a histone acetyltransferase (HAT) to promote transcriptional activation. Has significant histone acetyltransferase activity with core histones (H3 and H4), and also with nucleosome core particles. Also acetylates non-histone proteins, such as ACLY. Inhibits cell-cycle progression and counteracts the mitogenic activity of the adenoviral oncoprotein E1A. In case of HIV-1 infection, it is recruited by the viral protein Tat. Regulates Tat's transactivating activity and may help inducing chromatin remodeling of proviral genes.<ref>PMID:8684459</ref> <ref>PMID:9707565</ref> <ref>PMID:10675335</ref> <ref>PMID:23932781</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/cm/1cm0_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=1cm0 ConSurf].
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<div style="clear:both"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Single protein]]
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[[Category: Large Structures]]
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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: Marmorstein, R.]]
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[[Category: Marmorstein R]]
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[[Category: Rojas, J.R.]]
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[[Category: Rojas JR]]
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[[Category: Trievel, R.C.]]
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[[Category: Trievel RC]]
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[[Category: Wang, L.]]
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[[Category: Wang L]]
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[[Category: COA]]
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[[Category: acetyltransferase]]
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[[Category: coactivator]]
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[[Category: coenzyme a]]
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[[Category: p300/cbp associated factor]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 16:23:11 2007''
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Current revision

CRYSTAL STRUCTURE OF THE PCAF/COENZYME-A COMPLEX

PDB ID 1cm0

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