8hte
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Crystal structure of an effector mutant in complex with ubiquitin== | |
| + | <StructureSection load='8hte' size='340' side='right'caption='[[8hte]], [[Resolution|resolution]] 2.31Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[8hte]] 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/Saccharomyces_cerevisiae_S288C Saccharomyces cerevisiae S288C]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8HTE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8HTE 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]] 2.307Å</td></tr> | ||
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=AR6:[(2R,3S,4R,5R)-5-(6-AMINOPURIN-9-YL)-3,4-DIHYDROXY-OXOLAN-2-YL]METHYL+[HYDROXY-[[(2R,3S,4R,5S)-3,4,5-TRIHYDROXYOXOLAN-2-YL]METHOXY]PHOSPHORYL]+HYDROGEN+PHOSPHATE'>AR6</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NCA:NICOTINAMIDE'>NCA</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</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=8hte FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8hte OCA], [https://pdbe.org/8hte PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8hte RCSB], [https://www.ebi.ac.uk/pdbsum/8hte PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8hte 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> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Ubiquitination plays essential roles in eukaryotic cellular processes. The effector protein CteC from Chromobacterium violaceum blocks host ubiquitination by mono-ADP-ribosylation of ubiquitin (Ub) at residue T66. However, the structural basis for this modification is unknown. Here we report three crystal structures of CteC in complexes with Ub, NAD(+) or ADP-ribosylated Ub, which represent different catalytic states of CteC in the modification. CteC adopts a special 'D-E' catalytic motif for catalysis and binds NAD(+) in a half-ligand binding mode. The specific recognition of Ub by CteC is determined by a relatively separate Ub-targeting domain and a long loop L6, not the classic ADP-ribosylating turn-turn loop. Structural analyses with biochemical results reveal that CteC represents a large family of poly (ADP-ribose) polymerase (PARP)-like ADP-ribosyltransferases, which harbors chimeric features from the R-S-E and H-Y-E classes of ADP-ribosyltransferases. The family of CteC-like ADP-ribosyltransferases has a common 'D-E' catalytic consensus and exists extensively in bacteria and eukaryotic microorganisms. | ||
| - | + | Molecular basis of threonine ADP-ribosylation of ubiquitin by bacterial ARTs.,Tan J, Xu Y, Wang X, Yan F, Xian W, Liu X, Chen Y, Zhu Y, Zhou Y Nat Chem Biol. 2023 Nov 9. doi: 10.1038/s41589-023-01475-3. PMID:37945894<ref>PMID:37945894</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 8hte" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Chromobacterium violaceum ATCC 12472]] | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Saccharomyces cerevisiae S288C]] | ||
| + | [[Category: Tan J]] | ||
| + | [[Category: Wang X]] | ||
| + | [[Category: Zhou Y]] | ||
| + | [[Category: Zhu Y]] | ||
Revision as of 07:28, 22 November 2023
Crystal structure of an effector mutant in complex with ubiquitin
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