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2mp2

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Revision as of 17:34, 15 August 2018

Solution structure of SUMO dimer in complex with SIM2-3 from RNF4

Structural highlights

2mp2 is a 3 chain structure with sequence from Human. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Gene:	SMT3B, SMT3H1, SUMO3 (HUMAN)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[SUMO3_HUMAN] Ubiquitin-like protein which can be covalently attached to target lysines either as a monomer or as a lysine-linked polymer. Does not seem to be involved in protein degradation and may function as an antagonist of ubiquitin in the degradation process. Plays a role in a number of cellular processes such as nuclear transport, DNA replication and repair, mitosis and signal transduction. Covalent attachment to its substrates requires prior activation by the E1 complex SAE1-SAE2 and linkage to the E2 enzyme UBE2I, and can be promoted by an E3 ligase such as PIAS1-4, RANBP2 or CBX4.^[1] ^[2] [RNF4_MOUSE] E3 ubiquitin-protein ligase which binds polysumoylated chains covalently attached to proteins and mediates 'Lys-6'-, 'Lys-11'-, 'Lys-48'- and 'Lys-63'-linked polyubiquitination of those substrates and their subsequent targeting to the proteasome for degradation. Regulates the degradation of several proteins including PML and the transcriptional activator PEA3. Involved in chromosome alignment and spindle assembly, it regulates the kinetochore CENPH-CENPI-CENPK complex by targeting polysumoylated CENPI to proteasomal degradation. Regulates the cellular responses to hypoxia and heat shock through degradation of respectively EPAS1 and PARP1. Alternatively, it may also bind DNA/nucleosomes and have a more direct role in the regulation of transcription for instance enhancing basal transcription and steroid receptor-mediated transcriptional activation.^[3]

Publication Abstract from PubMed

The small ubiquitin-like modifier (SUMO) can form polymeric chains that are important signals in cellular processes such as meiosis, genome maintenance and stress response. The SUMO-targeted ubiquitin ligase RNF4 engages with SUMO chains on linked substrates and catalyses their ubiquitination, which targets substrates for proteasomal degradation. Here we use a segmental labelling approach combined with solution nuclear magnetic resonance (NMR) spectroscopy and biochemical characterization to reveal how RNF4 manipulates the conformation of the SUMO chain, thereby facilitating optimal delivery of the distal SUMO domain for ubiquitin transfer.

Structural insight into SUMO chain recognition and manipulation by the ubiquitin ligase RNF4.,Xu Y, Plechanovova A, Simpson P, Marchant J, Leidecker O, Kraatz S, Hay RT, Matthews SJ Nat Commun. 2014 Jun 27;5:4217. doi: 10.1038/ncomms5217. PMID:24969970^[4]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Tatham MH, Jaffray E, Vaughan OA, Desterro JM, Botting CH, Naismith JH, Hay RT. Polymeric chains of SUMO-2 and SUMO-3 are conjugated to protein substrates by SAE1/SAE2 and Ubc9. J Biol Chem. 2001 Sep 21;276(38):35368-74. Epub 2001 Jul 12. PMID:11451954 doi:10.1074/jbc.M104214200
↑ Meulmeester E, Kunze M, Hsiao HH, Urlaub H, Melchior F. Mechanism and consequences for paralog-specific sumoylation of ubiquitin-specific protease 25. Mol Cell. 2008 Jun 6;30(5):610-9. doi: 10.1016/j.molcel.2008.03.021. PMID:18538659 doi:10.1016/j.molcel.2008.03.021
↑ Liew CW, Sun H, Hunter T, Day CL. RING domain dimerization is essential for RNF4 function. Biochem J. 2010 Oct 1;431(1):23-9. PMID:20681948 doi:10.1042/BJ20100957
↑ Xu Y, Plechanovova A, Simpson P, Marchant J, Leidecker O, Kraatz S, Hay RT, Matthews SJ. Structural insight into SUMO chain recognition and manipulation by the ubiquitin ligase RNF4. Nat Commun. 2014 Jun 27;5:4217. doi: 10.1038/ncomms5217. PMID:24969970 doi:http://dx.doi.org/10.1038/ncomms5217

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 See Also
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2mp2"

@@ Line 1: / Line 1: @@
 ==Solution structure of SUMO dimer in complex with SIM2-3 from RNF4==
 <StructureSection load='2mp2' size='340' side='right' caption='[[2mp2]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2mp2]] is a 3 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MP2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2MP2 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2mp2]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MP2 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2MP2 FirstGlance]. <br>
-</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2mp2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mp2 OCA], [http://pdbe.org/2mp2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2mp2 RCSB], [http://www.ebi.ac.uk/pdbsum/2mp2 PDBsum]</span></td></tr>
+</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SMT3B, SMT3H1, SUMO3 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2mp2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mp2 OCA], [http://pdbe.org/2mp2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2mp2 RCSB], [http://www.ebi.ac.uk/pdbsum/2mp2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2mp2 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 23: / Line 25: @@
 __TOC__
 </StructureSection>
+[[Category: Human]]
 [[Category: Hay, R T]]
 [[Category: Leidecker, O]]

2mp2

From Proteopedia

Revision as of 17:34, 15 August 2018

Solution structure of SUMO dimer in complex with SIM2-3 from RNF4

Structural highlights

Function

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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