8htc
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of a SeMet-labeled effector from Chromobacterium violaceum in complex with Ubiquitin== | |
| - | + | <StructureSection load='8htc' size='340' side='right'caption='[[8htc]], [[Resolution|resolution]] 2.20Å' scene=''> | |
| - | + | == Structural highlights == | |
| - | + | <table><tr><td colspan='2'>[[8htc]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Chromobacterium_violaceum_ATCC_12472 Chromobacterium violaceum ATCC 12472] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8HTC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8HTC 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]] 2.2Å</td></tr> | |
| - | [[Category: | + | <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=8htc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8htc OCA], [https://pdbe.org/8htc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8htc RCSB], [https://www.ebi.ac.uk/pdbsum/8htc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8htc ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/CTEC_CHRVO CTEC_CHRVO] ADP-ribosyltransferase that specifically modifies host ubiquitin on 'Thr-66' residue, which causes the shutdown of polyubiquitin synthesis and disrupts the recognition and reversal of polyubiquitin in host cells during infection (PubMed:32330457). Threonine ADP-ribosylation of ubiquitin prevents the transfer of ubiquitin from ubiquitin-activating enzyme E1 to ubiquitin-conjugating enzyme E2, which inhibits subsequent ubiquitin activation and leads to the shutdown of polyubiquitin synthesis in host cells (PubMed:32330457). The modification also causes dysfunction of polyubiquitin chains in cells, thereby blocking host ubiquitin signaling (PubMed:32330457). ADP-ribosylation by CteC is likely irreversible (PubMed:32330457). Plays a crucial role in bacterial colonization in mice during infection (PubMed:32330457).<ref>PMID:32330457</ref> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Chromobacterium violaceum ATCC 12472]] | ||
| + | [[Category: Homo sapiens]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Tan J]] | ||
| + | [[Category: Wang X]] | ||
| + | [[Category: Zhou Y]] | ||
| + | [[Category: Zhu Y]] | ||
Current revision
Crystal structure of a SeMet-labeled effector from Chromobacterium violaceum in complex with Ubiquitin
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