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[[Image:2rsd.jpg|left|200px]]
==Solution structure of the plant homeodomain (PHD) of the E3 SUMO ligase Siz1 from rice==
<StructureSection load='2rsd' size='340' side='right' caption='[[2rsd]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2rsd]] is a 1 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2RSD FirstGlance]. <br>
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene><br>
<tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SIZ1, Os05g0125000, LOC_Os05g03430, OSJNBb0079L11.3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=39947 Oryza sativa Japonica Group])</td></tr>
<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=2rsd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2rsd OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2rsd RCSB], [http://www.ebi.ac.uk/pdbsum/2rsd PDBsum]</span></td></tr>
<table>
<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.


{{STRUCTURE_2rsd|  PDB=2rsd  |  SCENE=  }}
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>


===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>
{{ABSTRACT_PUBMED_22626555}}
== References ==
 
<references/>
==About this Structure==
__TOC__
[[2rsd]] is a 1 chain structure with sequence from [http://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].
</StructureSection>
 
==Reference==
<ref group="xtra">PMID:022626555</ref><references group="xtra"/>
[[Category: Oryza sativa japonica group]]
[[Category: Oryza sativa japonica group]]
[[Category: Shindo, H.]]
[[Category: Shindo, H.]]
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