View source for 6uyp


==Crystal structure of K39-acetylated SUMO1 in complex with PML-SIM==
<StructureSection load='6uyp' size='340' side='right'caption='[[6uyp]], [[Resolution|resolution]] 1.42&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6uyp]] is a 2 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=6UYP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6UYP 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]] 1.418&#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></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=6uyp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6uyp OCA], [https://pdbe.org/6uyp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6uyp RCSB], [https://www.ebi.ac.uk/pdbsum/6uyp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6uyp ProSAT]</span></td></tr>
</table>
== Disease ==
[https://www.uniprot.org/uniprot/PML_HUMAN PML_HUMAN] Note=A chromosomal aberration involving PML may be a cause of acute promyelocytic leukemia (APL). Translocation t(15;17)(q21;q21) with RARA. The PML breakpoints (type A and type B) lie on either side of an alternatively spliced exon.<ref>PMID:1652369</ref> <ref>PMID:1720570</ref> 
== Function ==
[https://www.uniprot.org/uniprot/PML_HUMAN PML_HUMAN] Key component of PML nuclear bodies that regulate a large number of cellular processes by facilitating post-translational modification of target proteins, promoting protein-protein contacts, or by sequestering proteins. Functions as tumor suppressor. Required for normal, caspase-dependent apoptosis in response to DNA damage, FAS, TNF, or interferons. Plays a role in transcription regulation, DNA damage response, DNA repair and chromatin organization. Plays a role in processes regulated by retinoic acid, regulation of cell division, terminal differentiation of myeloid precursor cells and differentiation of neural progenitor cells. Required for normal immunity to microbial infections. Plays a role in antiviral response. In the cytoplasm, plays a role in TGFB1-dependent processes. Regulates p53/TP53 levels by inhibiting its ubiquitination and proteasomal degradation. Regulates activation of p53/TP53 via phosphorylation at 'Ser-20'. Sequesters MDM2 in the nucleolus after DNA damage, and thereby inhibits ubiquitination and degradation of p53/TP53. Regulates translation of HIF1A by sequestering MTOR, and thereby plays a role in neoangiogenesis and tumor vascularization. Regulates RB1 phosphorylation and activity. Required for normal development of the brain cortex during embryogenesis. Can sequester herpes virus and varicella virus proteins inside PML bodies, and thereby inhibit the formation of infectious viral particles. Regulates phosphorylation of ITPR3 and plays a role in the regulation of calcium homeostasis at the endoplasmic reticulum (By similarity). Regulates transcription activity of ELF4. Inhibits specifically the activity of the tetrameric form of PKM. Together with SATB1, involved in local chromatin-loop remodeling and gene expression regulation at the MHC-I locus. Regulates PTEN compartmentalization through the inhibition of USP7-mediated deubiquitination.<ref>PMID:9756909</ref> <ref>PMID:10610177</ref> <ref>PMID:10684855</ref> <ref>PMID:11025664</ref> <ref>PMID:11432836</ref> <ref>PMID:12402044</ref> <ref>PMID:12439746</ref> <ref>PMID:12810724</ref> <ref>PMID:14976184</ref> <ref>PMID:15195100</ref> <ref>PMID:15356634</ref> <ref>PMID:17030982</ref> <ref>PMID:18298799</ref> <ref>PMID:18716620</ref> <ref>PMID:17173041</ref> <ref>PMID:19567472</ref> <ref>PMID:21172801</ref> <ref>PMID:21304940</ref> 
<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 6uyp" 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]]