4gf1: Difference between revisions
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[[ | ==Crystal Structure of Certhrax== | ||
<StructureSection load='4gf1' size='340' side='right' caption='[[4gf1]], [[Resolution|resolution]] 2.25Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4gf1]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bacillus_cereus Bacillus cereus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4GF1 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4GF1 FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=UNX:UNKNOWN+ATOM+OR+ION'>UNX</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4fxq|4fxq]], [[4fk7|4fk7]]</td></tr> | |||
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BCE_G9241_pBC218_0027 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1396 Bacillus cereus])</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=4gf1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4gf1 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4gf1 RCSB], [http://www.ebi.ac.uk/pdbsum/4gf1 PDBsum]</span></td></tr> | |||
</table> | |||
<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. | |||
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> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
== | __TOC__ | ||
</StructureSection> | |||
[[Category: Bacillus cereus]] | [[Category: Bacillus cereus]] | ||
[[Category: Arrowsmith, C H | [[Category: Arrowsmith, C H]] | ||
[[Category: Bountra, C | [[Category: Bountra, C]] | ||
[[Category: Dimov, S | [[Category: Dimov, S]] | ||
[[Category: Edwards, A M | [[Category: Edwards, A M]] | ||
[[Category: Hong, B S | [[Category: Hong, B S]] | ||
[[Category: Park, H | [[Category: Park, H]] | ||
[[Category: | [[Category: Structural genomic]] | ||
[[Category: Tempel, W | [[Category: Tempel, W]] | ||
[[Category: Adp-ribosyltransferase]] | [[Category: Adp-ribosyltransferase]] | ||
[[Category: Transferase]] | [[Category: Transferase]] | ||
