2ebh
From Proteopedia
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= toxA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=747 Pasteurella multocida]) | |GENE= toxA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=747 Pasteurella multocida]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[2ebf|2EBF]], [[2ec5|2EC5]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2ebh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ebh OCA], [http://www.ebi.ac.uk/pdbsum/2ebh PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2ebh RCSB]</span> | ||
}} | }} | ||
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[[Category: Kamitani, S.]] | [[Category: Kamitani, S.]] | ||
[[Category: Kitadokoro, K.]] | [[Category: Kitadokoro, K.]] | ||
| - | [[Category: TRE]] | ||
[[Category: cys1165ser mutant]] | [[Category: cys1165ser mutant]] | ||
[[Category: inactivated mutant]] | [[Category: inactivated mutant]] | ||
[[Category: pasteurella multocida toxin]] | [[Category: pasteurella multocida toxin]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:46:32 2008'' |
Revision as of 23:46, 30 March 2008
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| , resolution 2.40Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | toxA (Pasteurella multocida) | ||||||
| Related: | 2EBF, 2EC5
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Crystal structures reveal a thiol-protease like catalytic triad in the C-terminal region of Pasteurella multocida toxin
Overview
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.
About this Structure
2EBH is a Single protein structure of sequence from Pasteurella multocida. Full crystallographic information is available from OCA.
Reference
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
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