3X0T : Crystal structure of PirA

  • A.H.J. Wang (Contributor)
  • Hao-Ching Wang (Contributor)
  • T.P. Ko (Contributor)
  • C. F. Lo (Contributor)



Experimental Technique/Method:X-RAY DIFFRACTION
Release Date:2015-08-26
Deposition Date:2014-10-22
Revision Date:
Molecular Weight:27892.35
Macromolecule Type:Protein
Residue Count:238
Atom Site Count:1895

Acute hepatopancreatic necrosis disease (AHPND) is a severe, newly emergent penaeid shrimp disease caused by Vibrio parahaemolyticus that has already led to tremendous losses in the cultured shrimp industry. Until now, its disease-causing mechanism has remained unclear. Here we show that an AHPND-causing strain of V. parahaemolyticus contains a 70-kbp plasmid (pVA1) with a postsegregational killing system, and that the ability to cause disease is abolished by the natural absence or experimental deletion of the plasmid-encoded homologs of the Photorhabdus insect-related (Pir) toxins PirA and PirB. We determined the crystal structure of the V. parahaemolyticus PirA and PirB (PirA(vp) and PirB(vp)) proteins and found that the overall structural topology of PirA(vp)/PirB(vp) is very similar to that of the Bacillus Cry insecticidal toxin-like proteins, despite the low sequence identity (<10%). This structural similarity suggests that the putative PirAB(vp) heterodimer might emulate the functional domains of the Cry protein, and in particular its pore-forming activity. The gene organization of pVA1 further suggested that pirAB(vp) may be lost or acquired by horizontal gene transfer via transposition or homologous recombination.
可用日期8月 26 2015
發行者Unknown Publisher