Structural highlights
Publication Abstract from PubMed
Helicobacter pylori neutrophil-activating protein (HP-NAP) is a Dps-like iron storage protein forming a dodecameric shell, and promotes adhesion of neutrophils to endothelial cells. The crystal structure of HP-NAP in a Zn(2+)- or Cd(2+)-bound form reveals the binding of two zinc or two cadmium ions and their bridged water molecule at the ferroxidase center (FOC). The two zinc ions are coordinated in a tetrahedral manner to the conserved residues among HP-NAP and Dps proteins. The two cadmium ions are coordinated in a trigonal-bipyramidal and distorted octahedral manner. In both structures, the second ion is more weakly coordinated than the first. Another zinc ion is found inside of the negatively-charged threefold-related pore, which is suitable for metal ions to pass through.
Crystal structure of Helicobacter pylori neutrophil-activating protein with a di-nuclear ferroxidase center in a zinc or cadmium-bound form.,Yokoyama H, Tsuruta O, Akao N, Fujii S Biochem Biophys Res Commun. 2012 Jun 15;422(4):745-50. Epub 2012 May 19. PMID:22618234[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Yokoyama H, Tsuruta O, Akao N, Fujii S. Crystal structure of Helicobacter pylori neutrophil-activating protein with a di-nuclear ferroxidase center in a zinc or cadmium-bound form. Biochem Biophys Res Commun. 2012 Jun 15;422(4):745-50. Epub 2012 May 19. PMID:22618234 doi:10.1016/j.bbrc.2012.05.073
