5jp1: Difference between revisions
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<StructureSection load='5jp1' size='340' side='right'caption='[[5jp1]], [[Resolution|resolution]] 2.10Å' scene=''> | <StructureSection load='5jp1' size='340' side='right'caption='[[5jp1]], [[Resolution|resolution]] 2.10Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5jp1]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JP1 OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[5jp1]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Solanum_lycopersicum Solanum lycopersicum] and [https://en.wikipedia.org/wiki/Xanthomonas_campestris_pv._vesicatoria_str._85-10 Xanthomonas campestris pv. vesicatoria str. 85-10]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JP1 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5JP1 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.1Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AYE:PROP-2-EN-1-AMINE'>AYE</scene>, <scene name='pdbligand=D1D:(4S,5S)-1,2-DITHIANE-4,5-DIOL'>D1D</scene>, <scene name='pdbligand=MLI:MALONATE+ION'>MLI</scene></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=5jp1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jp1 OCA], [https://pdbe.org/5jp1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5jp1 RCSB], [https://www.ebi.ac.uk/pdbsum/5jp1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5jp1 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/Q3BYJ5_XANE5 Q3BYJ5_XANE5] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Solanum lycopersicum]] | ||
[[Category: | [[Category: Xanthomonas campestris pv. vesicatoria str. 85-10]] | ||
[[Category: | [[Category: Komander D]] | ||
[[Category: | [[Category: Pruneda JN]] | ||
Latest revision as of 14:53, 6 November 2024
Structure of Xanthomonas campestris effector protein XopD bound to tomato SUMOStructure of Xanthomonas campestris effector protein XopD bound to tomato SUMO
Structural highlights
FunctionPublication Abstract from PubMedPathogenic bacteria rely on secreted effector proteins to manipulate host signaling pathways, often in creative ways. CE clan proteases, specific hydrolases for ubiquitin-like modifications (SUMO and NEDD8) in eukaryotes, reportedly serve as bacterial effector proteins with deSUMOylase, deubiquitinase, or, even, acetyltransferase activities. Here, we characterize bacterial CE protease activities, revealing K63-linkage-specific deubiquitinases in human pathogens, such as Salmonella, Escherichia, and Shigella, as well as ubiquitin/ubiquitin-like cross-reactive enzymes in Chlamydia, Rickettsia, and Xanthomonas. Five crystal structures, including ubiquitin/ubiquitin-like complexes, explain substrate specificities and redefine relationships across the CE clan. Importantly, this work identifies novel family members and provides key discoveries among previously reported effectors, such as the unexpected deubiquitinase activity in Xanthomonas XopD, contributed by an unstructured ubiquitin binding region. Furthermore, accessory domains regulate properties such as subcellular localization, as exemplified by a ubiquitin-binding domain in Salmonella Typhimurium SseL. Our work both highlights and explains the functional adaptations observed among diverse CE clan proteins. The Molecular Basis for Ubiquitin and Ubiquitin-like Specificities in Bacterial Effector Proteases.,Pruneda JN, Durkin CH, Geurink PP, Ovaa H, Santhanam B, Holden DW, Komander D Mol Cell. 2016 Jul 21;63(2):261-76. doi: 10.1016/j.molcel.2016.06.015. Epub 2016 , Jul 14. PMID:27425412[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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