9fn4: Difference between revisions

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'''Unreleased structure'''


The entry 9fn4 is ON HOLD
==DUBS Parachlamydia sp. PcJOS==
<StructureSection load='9fn4' size='340' side='right'caption='[[9fn4]], [[Resolution|resolution]] 2.15&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9fn4]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Parachlamydia_sp. Parachlamydia sp.]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9FN4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9FN4 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]] 2.15&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=TLA:L(+)-TARTARIC+ACID'>TLA</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=9fn4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9fn4 OCA], [https://pdbe.org/9fn4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9fn4 RCSB], [https://www.ebi.ac.uk/pdbsum/9fn4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9fn4 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A2H9SU66_9BACT A0A2H9SU66_9BACT]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Many intracellular bacteria secrete deubiquitinase (DUB) effectors into eukaryotic host cells to keep the bacterial surface or the enclosing vesicle membrane free of ubiquitin marks. This study describes a family of DUBs from several bacterial genera, including Simkania, Parachlamydia, Burkholderia, and Pigmentiphaga, which is structurally related to eukaryotic Josephin-type DUBs but contains members that catalyze a unique destructive substrate deubiquitination. These ubiquitin C-terminal clippases (UCCs) cleave ubiquitin before the C-terminal diGly motif, thereby truncating the modifier and leaving a remnant on the substrate. By comparing the crystal structures of substrate-bound clippases and a closely related conventional DUB, we identified the factors causing this shift and found them to be conserved in other clippases, including one highly specific for M1-linked ubiquitin chains. This enzyme class has great potential to serve as tools for studying the ubiquitin system, particularly aspects involving branched chains.


Authors:  
A family of bacterial Josephin-like deubiquitinases with an irreversible cleavage mode.,Hermanns T, Kolek S, Uthoff M, de Heiden RA, Mulder MPC, Baumann U, Hofmann K Mol Cell. 2025 Mar 20;85(6):1202-1215.e5. doi: 10.1016/j.molcel.2025.02.002. Epub , 2025 Mar 3. PMID:40037356<ref>PMID:40037356</ref>


Description:  
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
<div class="pdbe-citations 9fn4" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Parachlamydia sp]]
[[Category: Baumann U]]
[[Category: Hermanns T]]
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