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| | <StructureSection load='5wu0' size='340' side='right'caption='[[5wu0]], [[Resolution|resolution]] 2.25Å' scene=''> | | <StructureSection load='5wu0' size='340' side='right'caption='[[5wu0]], [[Resolution|resolution]] 2.25Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5wu0]] 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=5WU0 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=5WU0 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5wu0]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Clostridium_perfringens Clostridium perfringens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5WU0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5WU0 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAI:1,4-DIHYDRONICOTINAMIDE+ADENINE+DINUCLEOTIDE'>NAI</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]] 2.251Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5wtz|5wtz]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAI:1,4-DIHYDRONICOTINAMIDE+ADENINE+DINUCLEOTIDE'>NAI</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">becA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1502 "Bacillus perfringens" Veillon and Zuber 1898])</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=5wu0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wu0 OCA], [https://pdbe.org/5wu0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5wu0 RCSB], [https://www.ebi.ac.uk/pdbsum/5wu0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5wu0 ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=5wu0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5wu0 OCA], [http://pdbe.org/5wu0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5wu0 RCSB], [http://www.ebi.ac.uk/pdbsum/5wu0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5wu0 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | + | == Function == |
| | + | [https://www.uniprot.org/uniprot/X5I2D7_CLOPF X5I2D7_CLOPF] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacillus perfringens veillon and zuber 1898]] | + | [[Category: Clostridium perfringens]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Irikura, D]] | + | [[Category: Irikura D]] |
| - | [[Category: Toniti, W]] | + | [[Category: Toniti W]] |
| - | [[Category: Tsuge, H]] | + | [[Category: Tsuge H]] |
| - | [[Category: Tsurumura, T]] | + | [[Category: Tsurumura T]] |
| - | [[Category: Yoshida, T]] | + | [[Category: Yoshida T]] |
| - | [[Category: Actin]]
| + | |
| - | [[Category: Adp-ribosylation]]
| + | |
| - | [[Category: Bacterial toxin]]
| + | |
| - | [[Category: Cpile-a]]
| + | |
| - | [[Category: Toxin]]
| + | |
| Structural highlights
Function
X5I2D7_CLOPF
Publication Abstract from PubMed
Unusual outbreaks of food poisoning in Japan were reported in which Clostridium perfringens was strongly suspected to be the cause based on epidemiological information and fingerprinting of isolates. The isolated strains lack the typical C. perfringens enterotoxin (CPE) but secrete a new enterotoxin consisting of two components: C. perfringens iota-like enterotoxin-a (CPILE-a), which acts as an enzymatic ADP-ribosyltransferase, and CPILE-b, a membrane binding component. Here we present the crystal structures of apo-CPILE-a, NAD+-CPILE-a and NADH-CPILE-a. Though CPILE-a structure has high similarity with known iota toxin-a (Ia) with NAD+, it possesses two extra-long protruding loops from G262-S269 and E402-K408 that are distinct from Ia. Based on the Ia-actin complex structure, we focused on actin-binding interface regions (I-V) including two protruding loops (PT) and examined how mutations in these regions affect the ADP-ribosylation activity of CPILE-a. Though some site-directed mutagenesis studies have already been conducted on the actin binding site of Ia, in the present study, mutagenesis studies were conducted against both alpha- and beta/gamma-actin in CPILE-a and Ia. Interestingly, CPILE-a ADP-ribosylates both alpha- and beta/gamma-actin, but its sensitivity towards beta/gamma-actin is 36% compared with alpha-actin. Our results contrast to that only C2-I ADP-ribosylates beta/gamma-actin. We also showed that PT-I and two convex-concave interactions in CPILE-a are important for actin binding. The current study is the first detailed analysis of site-directed mutagenesis in the actin binding region of Ia and CPILE-a against both alpha- and beta/gamma-actin.
Crystal structure and structure-based mutagenesis of actin-specific ADP-ribosylating toxin CPILE-a as novel enterotoxin.,Toniti W, Yoshida T, Tsurumura T, Irikura D, Monma C, Kamata Y, Tsuge H PLoS One. 2017 Feb 15;12(2):e0171278. doi: 10.1371/journal.pone.0171278., eCollection 2017. PMID:28199340[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Toniti W, Yoshida T, Tsurumura T, Irikura D, Monma C, Kamata Y, Tsuge H. Crystal structure and structure-based mutagenesis of actin-specific ADP-ribosylating toxin CPILE-a as novel enterotoxin. PLoS One. 2017 Feb 15;12(2):e0171278. doi: 10.1371/journal.pone.0171278., eCollection 2017. PMID:28199340 doi:http://dx.doi.org/10.1371/journal.pone.0171278
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