View source for 6uyz


==Crystal structure of K46-acetylated SUMO1 in complex with phosphorylated DAXX==
<StructureSection load='6uyz' size='340' side='right'caption='[[6uyz]], [[Resolution|resolution]] 1.40&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6uyz]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6UYZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6UYZ FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.4&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ALY:N(6)-ACETYLLYSINE'>ALY</scene>, <scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</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=6uyz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6uyz OCA], [https://pdbe.org/6uyz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6uyz RCSB], [https://www.ebi.ac.uk/pdbsum/6uyz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6uyz ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The interactions between SUMO proteins and SUMO-interacting motif (SIM) in nuclear bodies formed by the promyelocytic leukemia (PML) protein (PML-NBs) have been shown to be modulated by either phosphorylation of the SIMs or acetylation of SUMO proteins. However, little is known about how this occurs at the atomic level. In this work, we examined the role that acetylation of SUMO1 plays on its binding to the phosphorylated SIMs (phosphoSIMs) of PML and Daxx. Our results demonstrate that SUMO1 binding to the phosphoSIM of either PML or Daxx is dramatically reduced by acetylation at either K39 or K46. However, acetylation at K37 only impacts binding to Daxx. Structures of acetylated SUMO1 variants bound to the phosphoSIMs of PML and Daxx demonstrate that there is structural plasticity in SUMO-SIM interactions. The plasticity observed in these structures provides a robust mechanism for regulating SUMO-SIM interactions in PML-NBs using signaling generated post-translational modifications.

Acetylation of SUMO1 Alters Interactions with the SIMs of PML and Daxx in a Protein-Specific Manner.,Mascle XH, Gagnon C, Wahba HM, Lussier-Price M, Cappadocia L, Sakaguchi K, Omichinski JG Structure. 2019 Dec 23. pii: S0969-2126(19)30437-X. doi:, 10.1016/j.str.2019.11.019. PMID:31879127<ref>PMID:31879127</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6uyz" style="background-color:#fffaf0;"></div>

==See Also==
*[[SUMO 3D Structures|SUMO 3D Structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Cappadocia L]]
[[Category: Gagnon C]]
[[Category: Lussier-Price M]]
[[Category: Mascle XH]]
[[Category: Omichinski JG]]
[[Category: Sakaguchi K]]
[[Category: Wahba HM]]