View source for 5h04


==Crystal structure of an ADP-ribosylating toxin BECa of a novel binary enterotoxin of C. perfringens with NADH==
<StructureSection load='5h04' size='340' side='right'caption='[[5h04]], [[Resolution|resolution]] 1.82&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5h04]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_perfringens"_veillon_and_zuber_1898 "bacillus perfringens" veillon and zuber 1898]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5H04 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5H04 FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAI:1,4-DIHYDRONICOTINAMIDE+ADENINE+DINUCLEOTIDE'>NAI</scene></td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5h03|5h03]]</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=5h04 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5h04 OCA], [http://pdbe.org/5h04 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5h04 RCSB], [http://www.ebi.ac.uk/pdbsum/5h04 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5h04 ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Binary enterotoxin of Clostridium perfringens (BEC), consisting of the components BECa and BECb, was recently identified as a novel enterotoxin produced by C. perfringens that causes acute gastroenteritis in humans. Although the detailed mechanism of cell intoxication by BEC remains to be defined, BECa shows both NAD+-glycohydrolase and actin ADP-ribosyltransferase activities in the presence of NAD+. In this study, we determined the first crystal structure of BECa in its apo-state and in complex with NADH. The structure of BECa shows striking resemblance with other binary actin ADP-ribosylating toxins (ADPRTs), especially in terms of its overall protein fold and mechanisms of substrate recognition. We present a detailed picture of interactions between BECa and NADH, including bound water molecules located near the C1'-N glycosidic bond of NADH and the catalytically important ADP-ribosylating turn-turn (ARTT) loop. We observed that the conformational rearrangement of the ARTT loop, possibly triggered by a conformational change involving a conserved tyrosine residue coupled with substrate binding, plays a crucial role in catalysis by properly positioning a catalytic glutamate residue in the E-X-E motif of the ARTT loop in contact with the nucleophile. Our results for BECa provide insight into the common catalytic mechanism of the family of binary actin ADPRTs.

Crystal structure of the ADP-ribosylating component of BEC, the binary enterotoxin of Clostridium perfringens.,Kawahara K, Yonogi S, Munetomo R, Oki H, Yoshida T, Kumeda Y, Matsuda S, Kodama T, Ohkubo T, Iida T, Nakamura S Biochem Biophys Res Commun. 2016 Nov 11;480(2):261-267. doi:, 10.1016/j.bbrc.2016.10.042. Epub 2016 Oct 15. PMID:27751850<ref>PMID:27751850</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5h04" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Bacillus perfringens veillon and zuber 1898]]
[[Category: Large Structures]]
[[Category: Iida, T]]
[[Category: Kawahara, K]]
[[Category: Kodama, T]]
[[Category: Kumeda, Y]]
[[Category: Matsuda, S]]
[[Category: Munetomo, R]]
[[Category: Nakamura, S]]
[[Category: Ohkubo, T]]
[[Category: Oki, H]]
[[Category: Yonogi, S]]
[[Category: Yoshida, T]]
[[Category: Adp-ribosyltransferase]]
[[Category: Toxin]]