6ups: Difference between revisions
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New page: '''Unreleased structure''' The entry 6ups is ON HOLD Authors: Ronau, J.A., Lim, C.S., Xiong, Y. Description: Crystal structure of the deubiquitylase domain from the Orientia tsutsugamu... |
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==Crystal structure of the deubiquitylase domain from the Orientia tsutsugamushi protein OTT_1962 (OtDUB)== | |||
<StructureSection load='6ups' size='340' side='right'caption='[[6ups]], [[Resolution|resolution]] 2.00Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[6ups]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Orientia_tsutsugamushi_str._Ikeda Orientia tsutsugamushi str. Ikeda]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6UPS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6UPS 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]] 2Å</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></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=6ups FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ups OCA], [https://pdbe.org/6ups PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ups RCSB], [https://www.ebi.ac.uk/pdbsum/6ups PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ups ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/B3CVM3_ORITI B3CVM3_ORITI] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Ubiquitin mediated signaling contributes critically to host cell defenses during pathogen infection. Many pathogens manipulate the ubiquitin system to evade these defenses. Here we characterize a likely effector protein bearing a deubiquitylase (DUB) domain from the obligate intracellular bacterium Orientia tsutsugamushi, the causative agent of scrub typhus. The Ulp1-like DUB prefers ubiquitin substrates over ubiquitin-like proteins and efficiently cleaves polyubiquitin chains of three or more ubiquitins. The co-crystal structure of the DUB (OtDUB) domain with ubiquitin revealed three bound ubiquitins: one engages the S1 site, the second binds an S2 site contributing to chain specificity and the third binds a unique ubiquitin-binding domain (UBD). The UBD modulates OtDUB activity, undergoes a pronounced structural transition upon binding ubiquitin, and binds monoubiquitin with an unprecedented ~5 nM dissociation constant. The characterization and high-resolution structure determination of this enzyme should aid in its development as a drug target to counter Orientia infections. | |||
A deubiquitylase with an unusually high-affinity ubiquitin-binding domain from the scrub typhus pathogen Orientia tsutsugamushi.,Berk JM, Lim C, Ronau JA, Chaudhuri A, Chen H, Beckmann JF, Loria JP, Xiong Y, Hochstrasser M Nat Commun. 2020 May 11;11(1):2343. doi: 10.1038/s41467-020-15985-4. PMID:32393759<ref>PMID:32393759</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
[[Category: | </div> | ||
[[Category: | <div class="pdbe-citations 6ups" style="background-color:#fffaf0;"></div> | ||
[[Category: Lim | == References == | ||
[[Category: Xiong | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Large Structures]] | |||
[[Category: Orientia tsutsugamushi str. Ikeda]] | |||
[[Category: Lim CS]] | |||
[[Category: Ronau JA]] | |||
[[Category: Xiong Y]] | |||
Latest revision as of 13:11, 6 November 2024
Crystal structure of the deubiquitylase domain from the Orientia tsutsugamushi protein OTT_1962 (OtDUB)
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