3tw1

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[[Image:3tw1.png|left|200px]]
 
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==Structure of Rtt106-AHN==
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The line below this paragraph, containing "STRUCTURE_3tw1", creates the "Structure Box" on the page.
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<StructureSection load='3tw1' size='340' side='right'caption='[[3tw1]], [[Resolution|resolution]] 1.77&Aring;' scene=''>
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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'>[[3tw1]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TW1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TW1 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]] 1.772&#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=AHN:N-[2-(1H-IMIDAZOL-4-YL)ETHYL]ACETAMIDE'>AHN</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr>
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{{STRUCTURE_3tw1| PDB=3tw1 | 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=3tw1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tw1 OCA], [https://pdbe.org/3tw1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3tw1 RCSB], [https://www.ebi.ac.uk/pdbsum/3tw1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3tw1 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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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Dynamic variations in the structure of chromatin influence virtually all DNA-related processes in eukaryotes and are controlled in part by post-translational modifications of histones. One such modification, the acetylation of lysine 56 (H3K56ac) in the amino-terminal alpha-helix (alphaN) of histone H3, has been implicated in the regulation of nucleosome assembly during DNA replication and repair, and nucleosome disassembly during gene transcription. In Saccharomyces cerevisiae, the histone chaperone Rtt106 contributes to the deposition of newly synthesized H3K56ac-carrying H3-H4 complex on replicating DNA, but it is unclear how Rtt106 binds H3-H4 and specifically recognizes H3K56ac as there is no apparent acetylated lysine reader domain in Rtt106. Here, we show that two domains of Rtt106 are involved in a combinatorial recognition of H3-H4. An N-terminal domain homodimerizes and interacts with H3-H4 independently of acetylation while a double pleckstrin-homology (PH) domain binds the K56-containing region of H3. Affinity is markedly enhanced upon acetylation of K56, an effect that is probably due to increased conformational entropy of the alphaN helix of H3. Our data support a mode of interaction where the N-terminal homodimeric domain of Rtt106 intercalates between the two H3-H4 components of the (H3-H4)(2) tetramer while two double PH domains in the Rtt106 dimer interact with each of the two H3K56ac sites in (H3-H4)(2). We show that the Rtt106-(H3-H4)(2) interaction is important for gene silencing and the DNA damage response.
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===Structure of Rtt106-AHN===
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Structural basis for recognition of H3K56-acetylated histone H3-H4 by the chaperone Rtt106.,Su D, Hu Q, Li Q, Thompson JR, Cui G, Fazly A, Davies BA, Botuyan MV, Zhang Z, Mer G Nature. 2012 Feb 5. doi: 10.1038/nature10861. PMID:22307274<ref>PMID:22307274</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_22307274}}, adds the Publication Abstract to the page
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<div class="pdbe-citations 3tw1" style="background-color:#fffaf0;"></div>
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(as it appears on PubMed at http://www.pubmed.gov), where 22307274 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_22307274}}
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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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[[3tw1]] 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=3TW1 OCA].
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[[Category: Saccharomyces cerevisiae S288C]]
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[[Category: Mer G]]
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==Reference==
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[[Category: Su D]]
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<ref group="xtra">PMID:022307274</ref><references group="xtra"/>
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[[Category: Thompson JR]]
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[[Category: Saccharomyces cerevisiae]]
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[[Category: Mer, G.]]
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[[Category: Su, D.]]
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[[Category: Thompson, J R.]]
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[[Category: Chaperone]]
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[[Category: Chromosomal protein]]
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[[Category: Nucleus]]
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[[Category: Phosphoprotein]]
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[[Category: Tandem pleckstrin-homology domain]]
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[[Category: Transcription]]
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[[Category: Transcription regulation]]
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Current revision

Structure of Rtt106-AHN

PDB ID 3tw1

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