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| | <StructureSection load='2ebh' size='340' side='right'caption='[[2ebh]], [[Resolution|resolution]] 2.40Å' scene=''> | | <StructureSection load='2ebh' size='340' side='right'caption='[[2ebh]], [[Resolution|resolution]] 2.40Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2ebh]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/"bacterium_multocidum"_lehmann_and_neumann_1899 "bacterium multocidum" lehmann and neumann 1899]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2EBH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2EBH FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2ebh]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pasteurella_multocida Pasteurella multocida]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2EBH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2EBH FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</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]] 2.4Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2ebf|2ebf]], [[2ec5|2ec5]]</div></td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GLC:ALPHA-D-GLUCOSE'>GLC</scene>, <scene name='pdbligand=PRD_900006:trehalose'>PRD_900006</scene></td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">toxA ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=747 "Bacterium multocidum" Lehmann and Neumann 1899])</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=2ebh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ebh OCA], [https://pdbe.org/2ebh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ebh RCSB], [https://www.ebi.ac.uk/pdbsum/2ebh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ebh 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=2ebh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ebh OCA], [https://pdbe.org/2ebh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ebh RCSB], [https://www.ebi.ac.uk/pdbsum/2ebh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ebh ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[https://www.uniprot.org/uniprot/TOXA_PASMD TOXA_PASMD]] This is a dermonecrotic toxin. This osteolytic toxin, induces bone resorption. Potent mitogen. This toxin is associated with the severe progressive form of the atrophic rhinitis, a major respiratory disease in pigs.
| + | [https://www.uniprot.org/uniprot/TOXA_PASMD TOXA_PASMD] This is a dermonecrotic toxin. This osteolytic toxin, induces bone resorption. Potent mitogen. This toxin is associated with the severe progressive form of the atrophic rhinitis, a major respiratory disease in pigs. |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bacterium multocidum lehmann and neumann 1899]] | |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Horiguchi, Y]] | + | [[Category: Pasteurella multocida]] |
| - | [[Category: Kamitani, S]] | + | [[Category: Horiguchi Y]] |
| - | [[Category: Kitadokoro, K]] | + | [[Category: Kamitani S]] |
| - | [[Category: Cys1165ser mutant]] | + | [[Category: Kitadokoro K]] |
| - | [[Category: Inactivated mutant]]
| + | |
| - | [[Category: Pasteurella multocida toxin]]
| + | |
| - | [[Category: Toxin]]
| + | |
| Structural highlights
Function
TOXA_PASMD This is a dermonecrotic toxin. This osteolytic toxin, induces bone resorption. Potent mitogen. This toxin is associated with the severe progressive form of the atrophic rhinitis, a major respiratory disease in pigs.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Pasteurella multocida toxin (PMT), one of the virulence factors produced by the bacteria, exerts its toxicity by up-regulating various signaling cascades downstream of the heterotrimeric GTPases Gq and G12/13 in an unknown fashion. Here, we present the crystal structure of the C-terminal region (residues 575-1,285) of PMT, which carries an intracellularly active moiety. The overall structure of C-terminal region of PMT displays a Trojan horse-like shape, composed of three domains with a "feet"-,"body"-, and "head"-type arrangement, which were designated C1, C2, and C3 from the N to the C terminus, respectively. The C1 domain, showing marked similarity in steric structure to the N-terminal domain of Clostridium difficile toxin B, was found to lead the toxin molecule to the plasma membrane. The C3 domain possesses the Cys-His-Asp catalytic triad that is organized only when the Cys is released from a disulfide bond. The steric alignment of the triad corresponded well to that of papain or other enzymes carrying Cys-His-Asp. PMT toxicities on target cells were completely abrogated when one of the amino acids constituting the triad was mutated. Our results indicate that PMT is an enzyme toxin carrying the cysteine protease-like catalytic triad dependent on the redox state and functions on the cytoplasmic face of the plasma membrane of target cells.
Crystal structures reveal a thiol protease-like catalytic triad in the C-terminal region of Pasteurella multocida toxin.,Kitadokoro K, Kamitani S, Miyazawa M, Hanajima-Ozawa M, Fukui A, Miyake M, Horiguchi Y Proc Natl Acad Sci U S A. 2007 Mar 20;104(12):5139-44. Epub 2007 Mar 14. PMID:17360394[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Kitadokoro K, Kamitani S, Miyazawa M, Hanajima-Ozawa M, Fukui A, Miyake M, Horiguchi Y. Crystal structures reveal a thiol protease-like catalytic triad in the C-terminal region of Pasteurella multocida toxin. Proc Natl Acad Sci U S A. 2007 Mar 20;104(12):5139-44. Epub 2007 Mar 14. PMID:17360394
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