3fss
From Proteopedia
(Difference between revisions)
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==Structure of the tandem PH domains of Rtt106== | ==Structure of the tandem PH domains of Rtt106== | ||
- | <StructureSection load='3fss' size='340' side='right' caption='[[3fss]], [[Resolution|resolution]] 1.43Å' scene=''> | + | <StructureSection load='3fss' size='340' side='right'caption='[[3fss]], [[Resolution|resolution]] 1.43Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
- | <table><tr><td colspan='2'>[[3fss]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[3fss]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3FSS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3FSS FirstGlance]. <br> |
- | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=MLA:MALONIC+ACID'>MLA</scene></td></tr> | + | </td></tr><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=MLA:MALONIC+ACID'>MLA</scene></td></tr> |
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene></td></tr> | ||
- | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">N1346, RTT106, YNL206C ([ | + | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">N1346, RTT106, YNL206C ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 ATCC 18824])</td></tr> |
- | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=3fss FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3fss OCA], [https://pdbe.org/3fss PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3fss RCSB], [https://www.ebi.ac.uk/pdbsum/3fss PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3fss ProSAT]</span></td></tr> |
</table> | </table> | ||
== Function == | == Function == | ||
- | [[ | + | [[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> |
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Atcc 18824]] | [[Category: Atcc 18824]] | ||
+ | [[Category: Large Structures]] | ||
[[Category: Mer, G]] | [[Category: Mer, G]] | ||
[[Category: Su, D]] | [[Category: Su, D]] |
Current revision
Structure of the tandem PH domains of Rtt106
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