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==Full-length Cholix toxin from Vibrio cholerae in complex with NAD== | ==Full-length Cholix toxin from Vibrio cholerae in complex with NAD== | ||
<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 [http://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[3q9o]] is a 1 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3Q9O FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NAD:NICOTINAMIDE-ADENINE-DINUCLEOTIDE'>NAD</scene></td></tr> | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2q5t|2q5t]], [[2q6m|2q6m]], [[3ess|3ess]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2q5t|2q5t]], [[2q6m|2q6m]], [[3ess|3ess]]</td></tr> | ||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">chxa, toxA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=666 | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">chxa, toxA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=666 "Bacillo virgola del Koch" Trevisan 1884])</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3q9o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3q9o OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3q9o RCSB], [http://www.ebi.ac.uk/pdbsum/3q9o PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3q9o FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3q9o OCA], [http://pdbe.org/3q9o PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3q9o RCSB], [http://www.ebi.ac.uk/pdbsum/3q9o PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3q9o ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/ | [[http://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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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 3q9o" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Bacillo virgola del koch trevisan 1884]] | ||
[[Category: Fieldhouse, R J]] | [[Category: Fieldhouse, R J]] | ||
[[Category: Jorgensen, R]] | [[Category: Jorgensen, R]] | ||
Revision as of 10:37, 5 August 2016
Full-length Cholix toxin from Vibrio cholerae in complex with NADFull-length Cholix toxin from Vibrio cholerae in complex with NAD
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 PubMedCertain 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 AlsoReferences
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