6ulh: Difference between revisions

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-'''Unreleased structure'''
-The entry 6ulh is ON HOLD  until Paper Publication
+==Structure of MavC in complex with its substrate in R3 spacegroup==
+<StructureSection load='6ulh' size='340' side='right'caption='[[6ulh]], [[Resolution|resolution]] 1.97&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6ULH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6ULH 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]] 1.968&#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=6ulh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ulh OCA], [https://pdbe.org/6ulh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ulh RCSB], [https://www.ebi.ac.uk/pdbsum/6ulh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ulh ProSAT]</span></td></tr>
+</table>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The bacterial effector MavC modulates the host immune response by blocking Ube2N activity employing an E1-independent ubiquitin ligation, catalyzing formation of a gamma-glutamyl-epsilon-Lys (Gln40(Ub)-Lys92(Ube2N)) isopeptide crosslink using a transglutaminase mechanism. Here we provide biochemical evidence in support of MavC targeting the activated, thioester-linked Ube2N~ubiquitin conjugate, catalyzing an intramolecular transglutamination reaction, covalently crosslinking the Ube2N and Ub subunits effectively inactivating the E2~Ub conjugate. Ubiquitin exhibits weak binding to MavC alone, but shows an increase in affinity when tethered to Ube2N in a disulfide-linked substrate that mimics the charged E2~Ub conjugate. Crystal structures of MavC in complex with the substrate mimic and crosslinked product provide insights into the reaction mechanism and underlying protein dynamics that favor transamidation over deamidation, while revealing a crucial role for the structurally unique insertion domain in substrate recognition. This work provides a structural basis of ubiquitination by transglutamination and identifies this enzyme's true physiological substrate.
-Authors:
+Legionella effector MavC targets the Ube2N~Ub conjugate for noncanonical ubiquitination.,Puvar K, Iyer S, Fu J, Kenny S, Negron Teron KI, Luo ZQ, Brzovic PS, Klevit RE, Das C Nat Commun. 2020 May 12;11(1):2365. doi: 10.1038/s41467-020-16211-x. PMID:32398758<ref>PMID:32398758</ref>
-Description:
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
+<div class="pdbe-citations 6ulh" 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/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
+[[Category: Das C]]
+[[Category: Iyer S]]
+[[Category: Puvar K]]