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1roc

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(New page: 200px<br /><applet load="1roc" size="450" color="white" frame="true" align="right" spinBox="true" caption="1roc, resolution 1.50&Aring;" /> '''Crystal structure of...)
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[[Image:1roc.gif|left|200px]]<br /><applet load="1roc" size="450" color="white" frame="true" align="right" spinBox="true"
 
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caption="1roc, resolution 1.50&Aring;" />
 
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'''Crystal structure of the histone deposition protein Asf1'''<br />
 
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==Overview==
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==Crystal structure of the histone deposition protein Asf1==
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BACKGROUND: Asf1 is a ubiquitous eukaryotic histone binding and deposition, protein that mediates nucleosome formation in vitro and is required for, genome stability in vivo. Studies in a variety of organisms have defined, Asf1's role as a histone chaperone during DNA replication through specific, interactions with histones H3/H4 and the histone deposition factor CAF-I., In addition to its role in replication, conserved interactions with, proteins involved in chromatin silencing, transcription, chromatin, remodeling, and DNA repair have also established Asf1 as an important, component of a number of chromatin assembly and modulation complexes., RESULTS: We demonstrate that the highly conserved N-terminal domain of S., cerevisiae Asf1 (Asf1N) is the core region that mediates all tested, functions of the full-length protein. The crystal structure of this core, domain, determined to 1.5 A resolution, reveals a compact, immunoglobulin-like beta sandwich fold topped by three helical linkers., The surface of Asf1 displays a conserved hydrophobic groove flanked on one, side by an area of strong electronegative surface potential. These regions, represent potential binding sites for histones and other interacting, proteins. The structural model also allowed us to interpret mutagenesis, studies of the human Asf1a/HIRA interaction and to functionally define the, region of Asf1 responsible for Hir1-dependent telomeric silencing in, budding yeast. CONCLUSIONS: The evolutionarily conserved, N-terminal 155, amino acids of histone deposition protein Asf1 are functional in vitro and, in vivo. This core region of Asf1 adopts a compact immunoglobulin-fold, structure with distinct surface characteristics, including a Hir protein, binding region required for gene silencing.
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<StructureSection load='1roc' size='340' side='right'caption='[[1roc]], [[Resolution|resolution]] 1.50&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1roc]] is a 1 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=1ROC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ROC 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]] 1.5&#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=BR:BROMIDE+ION'>BR</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=1roc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1roc OCA], [https://pdbe.org/1roc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1roc RCSB], [https://www.ebi.ac.uk/pdbsum/1roc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1roc 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/ro/1roc_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=1roc 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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1ROC is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with BR as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1ROC OCA].
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*[[Anti-silencing factor|Anti-silencing factor]]
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*[[Anti-silencing factor 3D structures|Anti-silencing factor 3D structures]]
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==Reference==
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== References ==
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Structure and function of the conserved core of histone deposition protein Asf1., Daganzo SM, Erzberger JP, Lam WM, Skordalakes E, Zhang R, Franco AA, Brill SJ, Adams PD, Berger JM, Kaufman PD, Curr Biol. 2003 Dec 16;13(24):2148-58. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=14680630 14680630]
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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]]
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[[Category: Single protein]]
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[[Category: Adams PD]]
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[[Category: Adams, P.D.]]
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[[Category: Berger JM]]
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[[Category: Berger, J.M.]]
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[[Category: Brill SJ]]
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[[Category: Brill, S.J.]]
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[[Category: Daganzo SM]]
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[[Category: Daganzo, S.M.]]
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[[Category: Erzberger JP]]
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[[Category: Erzberger, J.P.]]
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[[Category: Franco AA]]
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[[Category: Franco, A.A.]]
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[[Category: Kaufman PD]]
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[[Category: Kaufman, P.D.]]
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[[Category: Lam WM]]
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[[Category: Lam, W.M.]]
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[[Category: Skordalakes E]]
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[[Category: Skordalakes, E.]]
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[[Category: Zhang R]]
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[[Category: Zhang, R.]]
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[[Category: BR]]
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[[Category: beta-sandwich]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 01:44:59 2007''
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Current revision

Crystal structure of the histone deposition protein Asf1

PDB ID 1roc

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