8htd
From Proteopedia
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=8htd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8htd OCA], [https://pdbe.org/8htd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8htd RCSB], [https://www.ebi.ac.uk/pdbsum/8htd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8htd 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=8htd FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8htd OCA], [https://pdbe.org/8htd PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8htd RCSB], [https://www.ebi.ac.uk/pdbsum/8htd PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8htd ProSAT]</span></td></tr> | ||
</table> | </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;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == 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. | 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. | + | 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. 2024 Apr;20(4):463-472. doi: 10.1038/s41589-023-01475-3. Epub 2023 , Nov 9. PMID:37945894<ref>PMID:37945894</ref> |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 8htd" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 8htd" style="background-color:#fffaf0;"></div> | ||
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| + | ==See Also== | ||
| + | *[[3D structures of ubiquitin|3D structures of ubiquitin]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
Current revision
Crystal structure of an effector from Chromobacterium violaceum in complex with ubiquitin
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