3q9o
From Proteopedia
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| - | [[ | + | ==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=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3q9o]] is a 1 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3Q9O FirstGlance]. <br> | ||
| + | </td></tr><tr><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><br> | ||
| + | <tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2q5t|2q5t]], [[2q6m|2q6m]], [[3ess|3ess]]</td></tr> | ||
| + | <tr><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 Vibrio cholerae])</td></tr> | ||
| + | <tr><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> | ||
| + | <table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == 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<ref>PMID:22535961</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
| - | + | == References == | |
| - | + | <references/> | |
| - | + | __TOC__ | |
| - | + | </StructureSection> | |
| - | + | ||
| - | == | + | |
| - | < | + | |
[[Category: Vibrio cholerae]] | [[Category: Vibrio cholerae]] | ||
[[Category: Fieldhouse, R J.]] | [[Category: Fieldhouse, R J.]] | ||
Revision as of 05:29, 4 June 2014
Full-length Cholix toxin from Vibrio cholerae in complex with NAD
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