This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


7p99

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (07:52, 1 May 2024) (edit) (undo)
 
Line 4: Line 4:
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[7p99]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Peromyscus_maniculatus_bairdii Peromyscus maniculatus bairdii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7P99 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7P99 FirstGlance]. <br>
<table><tr><td colspan='2'>[[7p99]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Peromyscus_maniculatus_bairdii Peromyscus maniculatus bairdii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7P99 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7P99 FirstGlance]. <br>
-
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8&#8491;</td></tr>
 +
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</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=7p99 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7p99 OCA], [https://pdbe.org/7p99 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7p99 RCSB], [https://www.ebi.ac.uk/pdbsum/7p99 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7p99 ProSAT]</span></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=7p99 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7p99 OCA], [https://pdbe.org/7p99 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7p99 RCSB], [https://www.ebi.ac.uk/pdbsum/7p99 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7p99 ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
-
[[https://www.uniprot.org/uniprot/A0A6J0CLW1_PERMB A0A6J0CLW1_PERMB]]
+
[https://www.uniprot.org/uniprot/A0A6J0CLW1_PERMB A0A6J0CLW1_PERMB]
-
<div style="background-color:#fffaf0;">
+
-
== Publication Abstract from PubMed ==
+
-
Post-translational protein modifications by ubiquitin and ubiquitin-like modifiers regulate many major pathways in the cell. These modifications can be reversed by de-ubiquitinating enzymes such as ubiquitin-specific proteases (USPs). Proteolytic activity towards ubiquitin-modified substrates is common to all USP family members except for USPL1, which shows a unique preference for the ubiquitin-like modifier SUMO. Here, we present the crystal structure of USPL1 bound to SUMO2, defining the key structural elements for the unusual deSUMOylase activity of USPL1. We identify specific contacts between SUMO2 and the USPL1 subdomains, including a unique hydrogen bond network of the SUMO2 C-terminal tail. In addition, we find that USPL1 lacks major structural elements present in all canonical USPs members such as the so-called blocking loops, which facilitates SUMO binding. Our data give insight into how a structural protein scaffold designed to bind ubiquitin has evolved to bind SUMO, providing an example of divergent evolution in the USP family.
+
-
 
+
-
Structural basis for the SUMO protease activity of the atypical ubiquitin-specific protease USPL1.,Li Y, Varejao N, Reverter D Nat Commun. 2022 Apr 5;13(1):1819. doi: 10.1038/s41467-022-29485-0. PMID:35383180<ref>PMID:35383180</ref>
+
-
 
+
-
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+
-
</div>
+
-
<div class="pdbe-citations 7p99" style="background-color:#fffaf0;"></div>
+
==See Also==
==See Also==
*[[SUMO 3D Structures|SUMO 3D Structures]]
*[[SUMO 3D Structures|SUMO 3D Structures]]
-
== References ==
 
-
<references/>
 
__TOC__
__TOC__
</StructureSection>
</StructureSection>

Current revision

Structure of human USPL1 in complex with SUMO2

PDB ID 7p99

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/7p99"
Personal tools