6kfp: Difference between revisions

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 <StructureSection load='6kfp' size='340' side='right'caption='[[6kfp]], [[Resolution|resolution]] 2.92&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[6kfp]] is a 3 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6KFP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6KFP FirstGlance]. <br>
+<table><tr><td colspan='2'>[[6kfp]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Legionella_pneumophila Legionella pneumophila]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6KFP OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6KFP FirstGlance]. <br>
-</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/E2_ubiquitin-conjugating_enzyme E2 ubiquitin-conjugating enzyme], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.3.2.23 2.3.2.23] </span></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.92&#8491;</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6kfp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6kfp OCA], [http://pdbe.org/6kfp PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6kfp RCSB], [http://www.ebi.ac.uk/pdbsum/6kfp PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6kfp ProSAT]</span></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=6kfp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6kfp OCA], [https://pdbe.org/6kfp PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6kfp RCSB], [https://www.ebi.ac.uk/pdbsum/6kfp PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6kfp ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/UBE2N_HUMAN UBE2N_HUMAN]] The UBE2V1-UBE2N and UBE2V2-UBE2N heterodimers catalyze the synthesis of non-canonical 'Lys-63'-linked polyubiquitin chains. This type of polyubiquitination does not lead to protein degradation by the proteasome. Mediates transcriptional activation of target genes. Plays a role in the control of progress through the cell cycle and differentiation. Plays a role in the error-free DNA repair pathway and contributes to the survival of cells after DNA damage. Acts together with the E3 ligases, HLTF and SHPRH, in the 'Lys-63'-linked poly-ubiquitination of PCNA upon genotoxic stress, which is required for DNA repair. Appears to act together with E3 ligase RNF5 in the 'Lys-63'-linked polyubiquitination of JKAMP thereby regulating JKAMP function by decreasing its association with components of the proteasome and ERAD. Promotes TRIM5 capsid-specific restriction activity and the UBE2V1-UBE2N heterodimer acts in concert with TRIM5 to generate 'Lys-63'-linked polyubiquitin chains which activate the MAP3K7/TAK1 complex which in turn results in the induction and expression of NF-kappa-B and MAPK-responsive inflammatory genes (By similarity).<ref>PMID:10089880</ref> <ref>PMID:14562038</ref> <ref>PMID:19269966</ref> <ref>PMID:20061386</ref> <ref>PMID:21512573</ref>
+[https://www.uniprot.org/uniprot/Q5ZTL4_LEGPH Q5ZTL4_LEGPH]
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Protein ubiquitination is one of the most prevalent post-translational modifications, controlling virtually every process in eukaryotic cells. Recently, the Legionella effector MavC was found to mediate a unique ubiquitination through transglutamination, linking ubiquitin (Ub) to UBE2N through Ub(Gln40) in a process that can be inhibited by another Legionella effector, Lpg2149. Here, we report the structures of MavC/UBE2N/Ub ternary complex, MavC/UBE2N-Ub (product) binary complex, and MavC/Lpg2149 binary complex. During the ubiquitination, the loop containing the modification site K92 of UBE2N undergoes marked conformational change, and Lpg2149 inhibits this ubiquitination through competing with Ub to bind MavC. Moreover, we found that MavC itself also exhibits weak deubiquitinase activity towards this non-canonical ubiquitination. Together, our study not only provides insights into the mechanism and inhibition of this transglutaminase-induced ubiquitination by MavC, but also sheds light on the future studies into UBE2N inhibition by this modification and deubiquitinases of this unique ubiquitination.
+Structural insights into the mechanism and inhibition of transglutaminase-induced ubiquitination by the Legionella effector MavC.,Mu Y, Wang Y, Huang Y, Li D, Han Y, Chang M, Fu J, Xie Y, Ren J, Wang H, Zhang Y, Luo ZQ, Feng Y Nat Commun. 2020 Apr 14;11(1):1774. doi: 10.1038/s41467-020-15645-7. PMID:32286321<ref>PMID:32286321</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 6kfp" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[3D structures of ubiquitin conjugating enzyme|3D structures of ubiquitin conjugating enzyme]]
 == References ==
 <references/>
 __TOC__
 </StructureSection>
-[[Category: E2 ubiquitin-conjugating enzyme]]
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
-[[Category: Feng, Y]]
+[[Category: Legionella pneumophila]]
-[[Category: Han, Y]]
+[[Category: Feng Y]]
-[[Category: Li, D]]
+[[Category: Han Y]]
-[[Category: Mu, Y]]
+[[Category: Li D]]
-[[Category: Wang, Y]]
+[[Category: Mu Y]]
-[[Category: Antitoxin]]
+[[Category: Wang Y]]
-[[Category: Antitoxin-transferase complex]]
-[[Category: Complex]]
-[[Category: Deamidase]]