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2hue

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(New page: 200px<br /><applet load="2hue" size="450" color="white" frame="true" align="right" spinBox="true" caption="2hue, resolution 1.7&Aring;" /> '''Structure of the H3-H...)
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[[Image:2hue.gif|left|200px]]<br /><applet load="2hue" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="2hue, resolution 1.7&Aring;" />
 
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'''Structure of the H3-H4 chaperone Asf1 bound to histones H3 and H4'''<br />
 
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==Overview==
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==Structure of the H3-H4 chaperone Asf1 bound to histones H3 and H4==
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Anti-silencing function 1 (Asf1) is a highly conserved chaperone of, histones H3/H4 that assembles or disassembles chromatin during, transcription, replication, and repair. The structure of the globular, domain of Asf1 bound to H3/H4 determined by X-ray crystallography to a, resolution of 1.7 Angstroms shows how Asf1 binds the H3/H4 heterodimer, enveloping the C terminus of histone H3 and physically blocking formation, of the H3/H4 heterotetramer. Unexpectedly, the C terminus of histone H4, that forms a mini-beta sheet with histone H2A in the nucleosome undergoes, a major conformational change upon binding to Asf1 and adds a beta strand, to the Asf1 beta sheet sandwich. Interactions with both H3 and H4 were, required for Asf1 histone chaperone function in vivo and in vitro. The, Asf1-H3/H4 structure suggests a "strand-capture" mechanism whereby the H4, tail acts as a lever to facilitate chromatin disassembly/assembly that may, be used ubiquitously by histone chaperones.
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<StructureSection load='2hue' size='340' side='right'caption='[[2hue]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[2hue]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] and [https://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HUE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HUE 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]] 1.7&#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=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</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=2hue FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hue OCA], [https://pdbe.org/2hue PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2hue RCSB], [https://www.ebi.ac.uk/pdbsum/2hue PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2hue ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/ASF1_YEAST ASF1_YEAST] Histone chaperone that facilitates histone deposition and histone exchange and removal during nucleosome assembly and disassembly. Facilitates histone deposition through both replication-dependent and replication-independent chromatin assembly pathways. Cooperates with chromatin assembly factor 1 (CAF-1) to promote replication-dependent chromatin assembly and with the HIR complex to promote replication-independent chromatin assembly, which may occur during transcription and DNA repair. May be required for the maintenance of a subset of replication elongation factors, including DNA polymerase epsilon, the RFC complex and PCNA, at stalled replication forks. Also required for acetylation of histone H3 on 'Lys-9' and 'Lys-56'.<ref>PMID:9290207</ref> <ref>PMID:10591219</ref> <ref>PMID:11412995</ref> <ref>PMID:11331602</ref> <ref>PMID:11731479</ref> <ref>PMID:11731480</ref> <ref>PMID:11404324</ref> <ref>PMID:11172707</ref> <ref>PMID:11856374</ref> <ref>PMID:11756556</ref> <ref>PMID:12093919</ref> <ref>PMID:14585955</ref> <ref>PMID:15071494</ref> <ref>PMID:15452122</ref> <ref>PMID:15175160</ref> <ref>PMID:15542829</ref> <ref>PMID:15542840</ref> <ref>PMID:15766286</ref> <ref>PMID:16303565</ref> <ref>PMID:15821127</ref> <ref>PMID:15901673</ref> <ref>PMID:16020781</ref> <ref>PMID:16143623</ref> <ref>PMID:16039596</ref> <ref>PMID:15632066</ref> <ref>PMID:15891116</ref> <ref>PMID:16141196</ref> <ref>PMID:15840725</ref> <ref>PMID:16815704</ref> <ref>PMID:16936140</ref> <ref>PMID:16582440</ref> <ref>PMID:16407267</ref> <ref>PMID:17046836</ref> <ref>PMID:16678113</ref> <ref>PMID:16501045</ref> <ref>PMID:16627621</ref> <ref>PMID:17107956</ref> <ref>PMID:17320445</ref> <ref>PMID:14680630</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/hu/2hue_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=2hue ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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2HUE is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] and [http://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis] with SO4, ZN and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2HUE OCA].
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*[[Anti-silencing factor 3D structures|Anti-silencing factor 3D structures]]
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*[[Histone|Histone]]
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==Reference==
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*[[Histone 3D structures|Histone 3D structures]]
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Structural basis for the histone chaperone activity of Asf1., English CM, Adkins MW, Carson JJ, Churchill ME, Tyler JK, Cell. 2006 Nov 3;127(3):495-508. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17081973 17081973]
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== References ==
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[[Category: Protein complex]]
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Large Structures]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Xenopus laevis]]
[[Category: Xenopus laevis]]
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[[Category: Churchill, M.E.A.]]
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[[Category: Churchill MEA]]
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[[Category: English, C.M]]
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[[Category: English CM]]
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[[Category: Tyler, J.K.]]
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[[Category: Tyler JK]]
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[[Category: GOL]]
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[[Category: SO4]]
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[[Category: ZN]]
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[[Category: elongated beta sandwhich]]
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[[Category: mini beta sheet]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 11:59:31 2007''
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Current revision

Structure of the H3-H4 chaperone Asf1 bound to histones H3 and H4

PDB ID 2hue

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