View source for 7oiy


==Crystal structure of the ZUFSP family member Mug105==
<StructureSection load='7oiy' size='340' side='right'caption='[[7oiy]], [[Resolution|resolution]] 2.05&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7oiy]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Schizosaccharomyces_pombe_972h- Schizosaccharomyces pombe 972h-]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7OIY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7OIY 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]] 2.05&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NA:SODIUM+ION'>NA</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=7oiy FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7oiy OCA], [https://pdbe.org/7oiy PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7oiy RCSB], [https://www.ebi.ac.uk/pdbsum/7oiy PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7oiy ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/MU105_SCHPO MU105_SCHPO] Deubiquitinase with endodeubiquitinase activity that preferentially cleaves 'Lys-48'-linked polyubiquitin chains (PubMed:29576528, PubMed:29476094). Shows only weak activity against 'Lys-63' and 'Lys-11'-linked chains (PubMed:29476094). Has a role in meiosis (PubMed:16303567).<ref>PMID:16303567</ref> <ref>PMID:29476094</ref> <ref>PMID:29576528</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Eukaryotic deubiquitinases are important regulators of ubiquitin signaling and can be subdivided into several structurally distinct classes. The ZUFSP family, with ZUP1 as its sole human member, has a modular architecture with a core catalytic domain highly active against the ubiquitin-derived peptide RLRGG, but not against ubiquitin itself. Ubiquitin recognition is conferred by additional non-catalytic domains, making full-length ZUP1 active against long K63-linked chains. However, non-mammalian ZUFSP family members contain different ubiquitin-binding domains in their N-terminal regions, despite their high conservation within the catalytic domain. Here, by working with representative ZUFSP family members from insects, fungi and plants, we show that different N-terminal domains are associated with different linkage preferences. Biochemical and structural studies suggest that the acquisition of two family-specific proximal domains have changed the default K48 preference of the ZUFSP family to the K63 preference observed in ZUP1 and its insect homolog. Additional N-terminal zinc finger domains promote chain cleavage without changing linkage-specificity.

A structural basis for the diverse linkage specificities within the ZUFSP deubiquitinase family.,Hermanns T, Pichlo C, Baumann U, Hofmann K Nat Commun. 2022 Jan 20;13(1):401. doi: 10.1038/s41467-022-28049-6. PMID:35058438<ref>PMID:35058438</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7oiy" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Schizosaccharomyces pombe 972h-]]
[[Category: Baumann U]]
[[Category: Hermanns T]]
[[Category: Hofmann K]]
[[Category: Pichlo C]]