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==Crystal structure of MvcA-UBE2N-Ub complex | ==Crystal structure of MvcA-UBE2N-Ub complex from Legionella pneumophila== | ||
<StructureSection load='6jky' size='340' side='right'caption='[[6jky]], [[Resolution|resolution]] 2.45Å' scene=''> | <StructureSection load='6jky' size='340' side='right'caption='[[6jky]], [[Resolution|resolution]] 2.45Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6jky]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6JKY OCA]. For a <b>guided tour on the structure components</b> use [ | <table><tr><td colspan='2'>[[6jky]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens], [https://en.wikipedia.org/wiki/Legionella_pneumophila_subsp._pneumophila_str._Philadelphia_1 Legionella pneumophila subsp. pneumophila str. Philadelphia 1] and [https://en.wikipedia.org/wiki/Schistosoma_margrebowiei Schistosoma margrebowiei]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6JKY OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6JKY 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]] 2.454Å</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=6jky FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6jky OCA], [https://pdbe.org/6jky PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6jky RCSB], [https://www.ebi.ac.uk/pdbsum/6jky PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6jky ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[ | [https://www.uniprot.org/uniprot/Q5ZTL3_LEGPH Q5ZTL3_LEGPH] | ||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The Legionella pneumophila effector MavC induces ubiquitination of the E2 ubiquitin-conjugating enzyme UBE2N by transglutamination, thereby abolishing its function in the synthesis of K63 -type polyubiquitin chains. The inhibition of UBE2N activity creates a conundrum because this E2 enzyme is important in multiple signaling pathways, including some that are important for intracellular L. pneumophila replication. Here, we show that prolonged inhibition of UBE2N activity by MavC restricts intracellular bacterial replication and that the activity of UBE2N is restored by MvcA, an ortholog of MavC (50% identity) with ubiquitin deamidase activity. MvcA functions to deubiquitinate UBE2N-Ub using the same catalytic triad required for its deamidase activity. Structural analysis of the MvcA-UBE2N-Ub complex reveals a crucial role of the insertion domain in MvcA in substrate recognition. Our study establishes a deubiquitination mechanism catalyzed by a deamidase, which, together with MavC, imposes temporal regulation of the activity of UBE2N during L. pneumophila infection. | |||
Legionella pneumophila regulates the activity of UBE2N by deamidase-mediated deubiquitination.,Gan N, Guan H, Huang Y, Yu T, Fu J, Nakayasu ES, Puvar K, Das C, Wang D, Ouyang S, Luo ZQ EMBO J. 2020 Feb 17;39(4):e102806. doi: 10.15252/embj.2019102806. Epub 2019 Dec, 11. PMID:31825121<ref>PMID:31825121</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 6jky" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[3D structures of ubiquitin|3D structures of ubiquitin]] | |||
*[[3D structures of ubiquitin conjugating enzyme|3D structures of ubiquitin conjugating enzyme]] | |||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Homo sapiens]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: | [[Category: Legionella pneumophila subsp. pneumophila str. Philadelphia 1]] | ||
[[Category: | [[Category: Schistosoma margrebowiei]] | ||
[[Category: | [[Category: Guan H]] | ||
[[Category: | [[Category: Ouyang SY]] | ||
Latest revision as of 13:14, 22 November 2023
Crystal structure of MvcA-UBE2N-Ub complex from Legionella pneumophilaCrystal structure of MvcA-UBE2N-Ub complex from Legionella pneumophila
Structural highlights
FunctionPublication Abstract from PubMedThe Legionella pneumophila effector MavC induces ubiquitination of the E2 ubiquitin-conjugating enzyme UBE2N by transglutamination, thereby abolishing its function in the synthesis of K63 -type polyubiquitin chains. The inhibition of UBE2N activity creates a conundrum because this E2 enzyme is important in multiple signaling pathways, including some that are important for intracellular L. pneumophila replication. Here, we show that prolonged inhibition of UBE2N activity by MavC restricts intracellular bacterial replication and that the activity of UBE2N is restored by MvcA, an ortholog of MavC (50% identity) with ubiquitin deamidase activity. MvcA functions to deubiquitinate UBE2N-Ub using the same catalytic triad required for its deamidase activity. Structural analysis of the MvcA-UBE2N-Ub complex reveals a crucial role of the insertion domain in MvcA in substrate recognition. Our study establishes a deubiquitination mechanism catalyzed by a deamidase, which, together with MavC, imposes temporal regulation of the activity of UBE2N during L. pneumophila infection. Legionella pneumophila regulates the activity of UBE2N by deamidase-mediated deubiquitination.,Gan N, Guan H, Huang Y, Yu T, Fu J, Nakayasu ES, Puvar K, Das C, Wang D, Ouyang S, Luo ZQ EMBO J. 2020 Feb 17;39(4):e102806. doi: 10.15252/embj.2019102806. Epub 2019 Dec, 11. PMID:31825121[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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