View source for 8cmr


==Linear specific OTU-type DUB SnOTU from the pathogen S. negenvensis in complex with linear di-ubiquitin==
<StructureSection load='8cmr' size='340' side='right'caption='[[8cmr]], [[Resolution|resolution]] 2.24&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8cmr]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Simkania_negevensis_Z Simkania negevensis Z]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8CMR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8CMR 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]] 2.24&#8491;</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=8cmr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8cmr OCA], [https://pdbe.org/8cmr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8cmr RCSB], [https://www.ebi.ac.uk/pdbsum/8cmr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8cmr ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/F8L9T9_SIMNZ F8L9T9_SIMNZ] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Besides the regulation of many cellular pathways, ubiquitination is important for defense against invading pathogens. Some intracellular bacteria have evolved deubiquitinase (DUB) effector proteins, which interfere with the host ubiquitin system and help the pathogen to evade xenophagy and lysosomal degradation. Most intracellular bacteria encode one or two DUBs, which are often linkage-promiscuous or preferentially cleave K63-linked chains attached to bacteria or bacteria-containing vacuoles. By contrast, the respiratory pathogen Legionella pneumophila possesses a much larger number of DUB effectors, including a K6-specific enzyme belonging to the OTU family and an M1-specific DUB uniquely found in this bacterium. Here, we report that the opportunistic pathogen Simkania negevensis, which is unrelated to Legionella but has a similar lifestyle, encodes a similarly large number of DUBs, including M1- and K6-specific enzymes. Simkania DUBs are highly diverse and include DUB classes never before seen in bacteria. Interestingly, the M1- and K6-specific DUBs of Legionella and Simkania are unrelated, suggesting that their acquisition occurred independently. We characterize the DUB activity of eight Simkania-encoded enzymes belonging to five different DUB classes. We also provide a structural basis for the M1-specificity of a Simkania DUB, which most likely evolved from a eukaryotic otubain-like precursor.

Functional and structural diversity in deubiquitinases of the Chlamydia-like bacterium Simkania negevensis.,Boll V, Hermanns T, Uthoff M, Erven I, Horner EM, Kozjak-Pavlovic V, Baumann U, Hofmann K Nat Commun. 2023 Nov 13;14(1):7335. doi: 10.1038/s41467-023-43144-y. PMID:37957213<ref>PMID:37957213</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 8cmr" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Simkania negevensis Z]]
[[Category: Baumann U]]
[[Category: Boll V]]
[[Category: Hermanns T]]
[[Category: Hofmann K]]
[[Category: Uthoff M]]