4fxq
From Proteopedia
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4fxq]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_cereus Bacillus cereus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FXQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4FXQ FirstGlance]. <br> | <table><tr><td colspan='2'>[[4fxq]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bacillus_cereus Bacillus cereus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4FXQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4FXQ FirstGlance]. <br> | ||
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=G9L:8-FLUORO-2-(3-PIPERIDIN-1-YLPROPANOYL)-1,3,4,5-TETRAHYDROBENZO[C][1,6]NAPHTHYRIDIN-6(2H)-ONE'>G9L</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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]] 1.9599Å</td></tr> |
| + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=G9L:8-FLUORO-2-(3-PIPERIDIN-1-YLPROPANOYL)-1,3,4,5-TETRAHYDROBENZO[C][1,6]NAPHTHYRIDIN-6(2H)-ONE'>G9L</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</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=4fxq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fxq OCA], [https://pdbe.org/4fxq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4fxq RCSB], [https://www.ebi.ac.uk/pdbsum/4fxq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4fxq 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=4fxq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4fxq OCA], [https://pdbe.org/4fxq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4fxq RCSB], [https://www.ebi.ac.uk/pdbsum/4fxq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4fxq ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[https://www.uniprot.org/uniprot/CRAX_BACCE CRAX_BACCE] A probable mono(ADP-ribosyl)transferase; it is not known which residue is targeted for ADP-ribosylation. Upon expression in yeast cells causes cell death.<ref>PMID:21170356</ref> | [https://www.uniprot.org/uniprot/CRAX_BACCE CRAX_BACCE] A probable mono(ADP-ribosyl)transferase; it is not known which residue is targeted for ADP-ribosylation. Upon expression in yeast cells causes cell death.<ref>PMID:21170356</ref> | ||
| - | <div style="background-color:#fffaf0;"> | ||
| - | == Publication Abstract from PubMed == | ||
| - | We identified Certhrax, the first anthrax-like mART toxin from the pathogenic G9241 strain of Bacillus cereus. Certhrax shares 31% sequence identity with anthrax lethal factor from Bacillus anthracis, however, we have shown that the toxicity of Certhrax resides in the mART domain, while anthrax uses a metalloprotease mechanism. Like anthrax lethal factor, Certhrax was found to require protective antigen for host cell entry. This two-domain enzyme was shown to be 60-fold more toxic to mammalian cells than anthrax lethal factor. Certhrax localizes to distinct regions within mouse RAW264.7 cells by 10 min post-infection and is extranuclear in its cellular location. Substitution of catalytic residues shows that the mART function is responsible for the toxicity, and it binds NAD+ with high affinity (KD = 52.3 +/- 12.2 muM). We report the 2.2 A Certhrax structure, highlighting its structural similarities and differences with anthrax lethal factor. We also determined the crystal structures of two good inhibitors (P6, KD = 1.7 +/- 0.2 muM, Ki = 1.8 +/- 0.4 muM; and PJ34, KD = 5.8 +/- 2.6 muM, Ki = 9.6 +/- 0.3 muM) in complex with Certhrax. As with other toxins in this family, the phosphate-nicotinamide loop moves toward the NAD+ binding site with bound inhibitor. These results indicate that Certhrax may be important in the pathogenesis of B. cereus. | ||
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| - | Certhrax toxin, an Anthrax-related ADP-ribosyltransferase from Bacillus cereus.,Visschedyk D, Rochon A, Tempel W, Dimov S, Park HW, Merrill AR J Biol Chem. 2012 Sep 19. PMID:22992735<ref>PMID:22992735</ref> | ||
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| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
| - | </div> | ||
| - | <div class="pdbe-citations 4fxq" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Current revision
Full-length Certhrax toxin from Bacillus cereus in complex with Inhibitor P6
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