7r2e

From Proteopedia

(Difference between revisions)

Revision as of 08:11, 7 December 2022

Structure of human Senp7 with SUMO2

Structural highlights

7r2e is a 4 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
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]

Publication Abstract from PubMed

SUMO proteases or deSUMOylases regulate the lifetime of SUMO-conjugated targets in the cell by cleaving off the isopetidic bond between the substrate and the SUMO modifier, thus reversing the conjugation activity of the SUMO E3 ligases. In humans the deSUMOylating activity is mainly conducted by the SENP/ULP protease family, which is constituted of six members sharing a homologous catalytic globular domain. SENP6 and SENP7 are the most divergent members of the family and they show a unique SUMO2/3 isoform preference and a particular activity for dismantling polySUMO2 chains. Here, we present the crystal structure of the catalytic domain of human SENP7 bound to SUMO2, revealing structural key elements for the SUMO2 isoform specificity of SENP7. In particular, we describe the specific contacts between SUMO2 and a unique insertion in SENP7 (named Loop1) that is responsible for the SUMO2 isoform specificity. All the other interface contacts between SENP7 and SUMO2, including the SUMO2 C-terminal tail interaction, are conserved among members of the SENP/ULP family. Our data give insight into an evolutionary adaptation to restrict the deSUMOylating activity in SENP6 and SENP7 for the SUMO2/3 isoforms.

Structural Basis for the SUMO2 Isoform Specificity of SENP7.,Li Y, De Bolos A, Amador V, Reverter D J Mol Biol. 2022 Dec 30;434(24):167875. doi: 10.1016/j.jmb.2022.167875. Epub 2022 , Nov 2. PMID:36334780^[3]

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
↑ Li Y, De Bolos A, Amador V, Reverter D. Structural Basis for the SUMO2 Isoform Specificity of SENP7. J Mol Biol. 2022 Dec 30;434(24):167875. doi: 10.1016/j.jmb.2022.167875. Epub 2022 , Nov 2. PMID:36334780 doi:http://dx.doi.org/10.1016/j.jmb.2022.167875

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/7r2e"

Categories: Homo sapiens | Large Structures | Li Y | Reverter D

@@ Line 1: / Line 1: @@
-'''Unreleased structure'''
-The entry 7r2e is ON HOLD  until 2024-02-04
+==Structure of human Senp7 with SUMO2==
+<StructureSection load='7r2e' size='340' side='right'caption='[[7r2e]], [[Resolution|resolution]] 1.74&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[7r2e]] 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=7R2E OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7R2E FirstGlance]. <br>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AYE:PROP-2-EN-1-AMINE'>AYE</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=7r2e FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7r2e OCA], [https://pdbe.org/7r2e PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7r2e RCSB], [https://www.ebi.ac.uk/pdbsum/7r2e PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7r2e ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/SUMO3_HUMAN 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.<ref>PMID:11451954</ref> <ref>PMID:18538659</ref>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+SUMO proteases or deSUMOylases regulate the lifetime of SUMO-conjugated targets in the cell by cleaving off the isopetidic bond between the substrate and the SUMO modifier, thus reversing the conjugation activity of the SUMO E3 ligases. In humans the deSUMOylating activity is mainly conducted by the SENP/ULP protease family, which is constituted of six members sharing a homologous catalytic globular domain. SENP6 and SENP7 are the most divergent members of the family and they show a unique SUMO2/3 isoform preference and a particular activity for dismantling polySUMO2 chains. Here, we present the crystal structure of the catalytic domain of human SENP7 bound to SUMO2, revealing structural key elements for the SUMO2 isoform specificity of SENP7. In particular, we describe the specific contacts between SUMO2 and a unique insertion in SENP7 (named Loop1) that is responsible for the SUMO2 isoform specificity. All the other interface contacts between SENP7 and SUMO2, including the SUMO2 C-terminal tail interaction, are conserved among members of the SENP/ULP family. Our data give insight into an evolutionary adaptation to restrict the deSUMOylating activity in SENP6 and SENP7 for the SUMO2/3 isoforms.
-Authors: Reverter, D., Li, Y.
+Structural Basis for the SUMO2 Isoform Specificity of SENP7.,Li Y, De Bolos A, Amador V, Reverter D J Mol Biol. 2022 Dec 30;434(24):167875. doi: 10.1016/j.jmb.2022.167875. Epub 2022 , Nov 2. PMID:36334780<ref>PMID:36334780</ref>
-Description: Structure of human Senp7 with SUMO2
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
-[[Category: Li, Y]]
+<div class="pdbe-citations 7r2e" style="background-color:#fffaf0;"></div>
-[[Category: Reverter, D]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Homo sapiens]]
+[[Category: Large Structures]]
+[[Category: Li Y]]
+[[Category: Reverter D]]

7r2e

From Proteopedia

Revision as of 08:11, 7 December 2022

Structure of human Senp7 with SUMO2

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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