3gyo

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{{Seed}}
 
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[[Image:3gyo.png|left|200px]]
 
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==Se-Met Rtt106p==
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The line below this paragraph, containing "STRUCTURE_3gyo", creates the "Structure Box" on the page.
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<StructureSection load='3gyo' size='340' side='right'caption='[[3gyo]], [[Resolution|resolution]] 3.10&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'>[[3gyo]] 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=3GYO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3GYO 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]] 3.1&#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=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
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{{STRUCTURE_3gyo| PDB=3gyo | 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=3gyo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3gyo OCA], [https://pdbe.org/3gyo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3gyo RCSB], [https://www.ebi.ac.uk/pdbsum/3gyo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3gyo ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/RT106_YEAST RT106_YEAST] Histones H3 and H4 chaperone involved in the nucleosome formation and heterochromatin silencing. Required for the deposition of H3K56ac-carrying H3-H4 complex onto newly-replicated DNA. Plays a role in the transcriptional regulation of the cell-cycle dependent histone genes by directly recruiting the SWI/SNF and RSC chromatin remodeling complexes to the histone genes in a cell cycle dependent manner. In cooperation with HIR and ASF1, creates a repressive structure at the core histone gene promoter and contributes to their repression outside of S phase. Involved in regulation of Ty1 transposition.<ref>PMID:11779788</ref> <ref>PMID:16157874</ref> <ref>PMID:17410207</ref> <ref>PMID:19683497</ref> <ref>PMID:20188666</ref> <ref>PMID:21763693</ref> <ref>PMID:22156209</ref> <ref>PMID:21444721</ref> <ref>PMID:21698254</ref> <ref>PMID:21978826</ref> <ref>PMID:22128187</ref> <ref>PMID:20007951</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/gy/3gyo_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=3gyo ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Rtt106p is a Saccharomyces cerevisiae histone chaperone with roles in heterochromatin silencing and nucleosome assembly. The molecular mechanism by which Rtt106p engages in chromatin dynamics remains unclear. Here, we report the 2.5 A crystal structure of the core domain of Rtt106p, which adopts an unusual "double pleckstrin homology" domain architecture that represents a novel structural mode for histone chaperones. A histone H3-H4-binding region and a novel double-stranded DNA-binding region have been identified. Mutagenesis studies reveal that the histone and DNA binding activities of Rtt106p are involved in Sir protein-mediated heterochromatin formation. Our results uncover the structural basis of the diverse functions of Rtt106p and provide new insights into its cellular roles.
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===Se-Met Rtt106p===
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Structural analysis of Rtt106p reveals a DNA binding role required for heterochromatin silencing.,Liu Y, Huang H, Zhou BO, Wang SS, Hu Y, Li X, Liu J, Zang J, Niu L, Wu J, Zhou JQ, Teng M, Shi Y J Biol Chem. 2010 Feb 5;285(6):4251-62. Epub 2009 Dec 10. PMID:20007951<ref>PMID:20007951</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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The line below this paragraph, {{ABSTRACT_PUBMED_20007951}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 3gyo" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 20007951 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_20007951}}
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__TOC__
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</StructureSection>
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==About this Structure==
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[[Category: Large Structures]]
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3GYO is a 1 chain structure with sequence 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=3GYO OCA].
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==Reference==
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<ref group="xtra">PMID:20007951</ref><references group="xtra"/>
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[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
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[[Category: Huang, H.]]
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[[Category: Huang H]]
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[[Category: Liu, Y.]]
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[[Category: Liu Y]]
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[[Category: Shi, Y.]]
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[[Category: Shi Y]]
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[[Category: Teng, M.]]
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[[Category: Teng M]]
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[[Category: Chaperone]]
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[[Category: Chromosomal protein]]
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[[Category: Histone chaperone]]
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[[Category: Nucleus]]
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[[Category: Phosphoprotein]]
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[[Category: Transcription]]
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[[Category: Transcription regulation]]
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[[Category: Transposition]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Feb 10 16:06:11 2010''
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Current revision

Se-Met Rtt106p

PDB ID 3gyo

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OCA

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