3to1

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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[3to1]] is a 2 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=3TO1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3TO1 FirstGlance]. <br>
<table><tr><td colspan='2'>[[3to1]] is a 2 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=3TO1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3TO1 FirstGlance]. <br>
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</td></tr><tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RTT106, YNL206C, N1346 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae])</td></tr>
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</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RTT106, YNL206C, N1346 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae])</td></tr>
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<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3to1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3to1 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3to1 RCSB], [http://www.ebi.ac.uk/pdbsum/3to1 PDBsum]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3to1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3to1 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3to1 RCSB], [http://www.ebi.ac.uk/pdbsum/3to1 PDBsum]</span></td></tr>
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<table>
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</table>
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== Function ==
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[[http://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>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
== Publication Abstract from PubMed ==
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Two surfaces on the histone chaperone Rtt106 mediate histone binding, replication, and silencing.,Zunder RM, Antczak AJ, Berger JM, Rine J Proc Natl Acad Sci U S A. 2011 Dec 23. PMID:22198837<ref>PMID:22198837</ref>
Two surfaces on the histone chaperone Rtt106 mediate histone binding, replication, and silencing.,Zunder RM, Antczak AJ, Berger JM, Rine J Proc Natl Acad Sci U S A. 2011 Dec 23. PMID:22198837<ref>PMID:22198837</ref>
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
</div>
== References ==
== References ==
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</StructureSection>
</StructureSection>
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
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[[Category: Antczak, A J.]]
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[[Category: Antczak, A J]]
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[[Category: Berger, J M.]]
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[[Category: Berger, J M]]
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[[Category: Rine, J.]]
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[[Category: Rine, J]]
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[[Category: Zunder, R M.]]
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[[Category: Zunder, R M]]
[[Category: Chaperone]]
[[Category: Chaperone]]
[[Category: Histone chaperone]]
[[Category: Histone chaperone]]

Revision as of 20:32, 25 December 2014

Two surfaces on Rtt106 mediate histone binding and chaperone activity

3to1, resolution 2.60Å

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