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| | <StructureSection load='3q9o' size='340' side='right'caption='[[3q9o]], [[Resolution|resolution]] 1.79Å' scene=''> | | <StructureSection load='3q9o' size='340' side='right'caption='[[3q9o]], [[Resolution|resolution]] 1.79Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[3q9o]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacillo_virgola_del_koch"_trevisan_1884 "bacillo virgola del koch" trevisan 1884]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3Q9O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3Q9O FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[3q9o]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Vibrio_cholerae Vibrio cholerae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3Q9O OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3Q9O FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene></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]] 1.793Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2q5t|2q5t]], [[2q6m|2q6m]], [[3ess|3ess]]</div></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">chxa, toxA ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=666 "Bacillo virgola del Koch" Trevisan 1884])</td></tr>
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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=3q9o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3q9o OCA], [https://pdbe.org/3q9o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3q9o RCSB], [https://www.ebi.ac.uk/pdbsum/3q9o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3q9o 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=3q9o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3q9o OCA], [https://pdbe.org/3q9o PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3q9o RCSB], [https://www.ebi.ac.uk/pdbsum/3q9o PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3q9o ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/CHXA_VIBCL CHXA_VIBCL]] An NAD-dependent ADP-ribosyltransferase (ADPRT), it catalyzes the transfer of the ADP-ribosyl moiety of oxidized NAD onto eukaryotic elongation factor 2 (eEF-2) thus arresting protein synthesis. It probably uses the eukaryotic prolow-density lipoprotein receptor-related protein 1 (LRP1) to enter mouse cells, although there seems to be at least one other receptor as well. Is active against mouse fibroblasts, Chinese hamster ovary eEF-2, brine shrimp (Artemia spp. nauplii) and upon expression in S.cerevisiae.<ref>PMID:18276581</ref> <ref>PMID:19793133</ref>
| + | [https://www.uniprot.org/uniprot/CHXA_VIBCL CHXA_VIBCL] An NAD-dependent ADP-ribosyltransferase (ADPRT), it catalyzes the transfer of the ADP-ribosyl moiety of oxidized NAD onto eukaryotic elongation factor 2 (eEF-2) thus arresting protein synthesis. It probably uses the eukaryotic prolow-density lipoprotein receptor-related protein 1 (LRP1) to enter mouse cells, although there seems to be at least one other receptor as well. Is active against mouse fibroblasts, Chinese hamster ovary eEF-2, brine shrimp (Artemia spp. nauplii) and upon expression in S.cerevisiae.<ref>PMID:18276581</ref> <ref>PMID:19793133</ref> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacillo virgola del koch trevisan 1884]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Fieldhouse, R J]] | + | [[Category: Vibrio cholerae]] |
| - | [[Category: Jorgensen, R]] | + | [[Category: Fieldhouse RJ]] |
| - | [[Category: Merrill, A R]] | + | [[Category: Jorgensen R]] |
| - | [[Category: Adp-ribosylating factor]] | + | [[Category: Merrill AR]] |
| - | [[Category: Alpha-beta complex]]
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| - | [[Category: Beta barrel]]
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| - | [[Category: Diphthamide on eukaryotic elongation factor 2]]
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| - | [[Category: Receptor binding domain]]
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| - | [[Category: Six alpha-helix bundle]]
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| - | [[Category: Transferase]]
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| - | [[Category: Translocation]]
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| Structural highlights
Function
CHXA_VIBCL An NAD-dependent ADP-ribosyltransferase (ADPRT), it catalyzes the transfer of the ADP-ribosyl moiety of oxidized NAD onto eukaryotic elongation factor 2 (eEF-2) thus arresting protein synthesis. It probably uses the eukaryotic prolow-density lipoprotein receptor-related protein 1 (LRP1) to enter mouse cells, although there seems to be at least one other receptor as well. Is active against mouse fibroblasts, Chinese hamster ovary eEF-2, brine shrimp (Artemia spp. nauplii) and upon expression in S.cerevisiae.[1] [2]
Publication Abstract from PubMed
Certain Vibrio cholerae strains produce cholix, a potent protein toxin that has diphthamide-specific ADP-ribosyltransferase activity against eukaryotic elongation factor 2. Here we present a 1.8A crystal structure of cholix in complex with its natural substrate, nicotinamide adenine dinucleotide (NAD+). We also substituted hallmark catalytic residues by site-directed mutagenesis and analyzed both NAD+ binding and ADPribosyltransferase activity using a fluorescence-based assay. These data are the basis for a new kinetic model of cholix toxin activity. Further, the new structural data serve as a reference for continuing inhibitor development for this toxin class.
The 1.8 angstrom cholix toxin crystal structure in complex with NAD and evidence for a new kinetic model.,Fieldhouse RJ, Jorgensen R, Lugo MR, Merrill AR J Biol Chem. 2012 Apr 25. PMID:22535961[3]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Jorgensen R, Purdy AE, Fieldhouse RJ, Kimber MS, Bartlett DH, Rod Merrill A. Cholix toxin, a novel ADP-ribosylating factor from vibrio cholerae. J Biol Chem. 2008 Feb 25;. PMID:18276581 doi:M710008200
- ↑ Turgeon Z, White D, Jorgensen R, Visschedyk D, Fieldhouse RJ, Mangroo D, Merrill AR. Yeast as a tool for characterizing mono-ADP-ribosyltransferase toxins. FEMS Microbiol Lett. 2009 Nov;300(1):97-106. Epub 2009 Aug 31. PMID:19793133 doi:10.1111/j.1574-6968.2009.01777.x
- ↑ Fieldhouse RJ, Jorgensen R, Lugo MR, Merrill AR. The 1.8 angstrom cholix toxin crystal structure in complex with NAD and evidence for a new kinetic model. J Biol Chem. 2012 Apr 25. PMID:22535961 doi:10.1074/jbc.M111.337311
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