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'''Unreleased structure'''


The entry 2rsd is ON HOLD
==Solution structure of the plant homeodomain (PHD) of the E3 SUMO ligase Siz1 from rice==
<StructureSection load='2rsd' size='340' side='right'caption='[[2rsd]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2rsd]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Oryza_sativa_Japonica_Group Oryza sativa Japonica Group]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2RSD OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2RSD FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2rsd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rsd OCA], [https://pdbe.org/2rsd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2rsd RCSB], [https://www.ebi.ac.uk/pdbsum/2rsd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2rsd ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/SIZ1_ORYSJ SIZ1_ORYSJ] Probable SUMO E3 ligase that may regulate Pi starvation responses (By similarity).
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
We determined the three-dimensional structure of the PHD finger of the rice Siz/PIAS-type SUMO ligase, OsSiz1, by NMR spectroscopy and investigated binding ability for a variety of methylated histone H3 tails, showing that OsSiz1-PHD primarily recognizes dimethylated Arg2 of the histone H3 and that methylations at Arg2 and Lys4 reveal synergy effect on binding to OsSiz1-PHD. The K4 cage of OsSiz1-PHD for trimethylated Lys4 of H3K4me3 was similar to that of the BPTF-PHD finger, while the R2 pocket for Arg2 was different. It is intriguing that the PHD module of Siz/PIAS plays an important role, with collaboration with the DNA binding domain SAP, in gene regulation through SUMOylation of a variety of effectors associated with the methylated arginine-riched chromatin domains.


Authors: Shindo, H., Tsuchiya, W., Suzuki, R., Yamazaki, T.
PHD finger of the SUMO ligase Siz/PIAS family in rice reveals specific binding for methylated histone H3 at lysine 4 and arginine 2.,Shindo H, Suzuki R, Tsuchiya W, Taichi M, Nishiuchi Y, Yamazaki T FEBS Lett. 2012 Jun 21;586(13):1783-9. Epub 2012 May 21. PMID:22626555<ref>PMID:22626555</ref>


Description: Solution structure of the plant homeodomain (PHD) of the E3 SUMO ligase Siz1 from rice
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2rsd" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Oryza sativa Japonica Group]]
[[Category: Shindo H]]
[[Category: Suzuki R]]
[[Category: Tsuchiya W]]
[[Category: Yamazaki T]]
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