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Crystal structure of Helicobacter pylori neutrophil-activating protein with a di-nuclear ferroxidase center in a zinc or cadmium-bound form.
Yokoyama, Hideshi; Tsuruta, Osamu; Akao, Naoya; Fujii, Satoshi.
Afiliación
  • Yokoyama H; School of Pharmaceutical Sciences, University of Shizuoka, 52-1 Yada, Shizuoka 422-8526, Japan. h-yokoya@u-shizuoka-ken.ac.jp
Biochem Biophys Res Commun ; 422(4): 745-50, 2012 Jun 15.
Article en En | MEDLINE | ID: mdl-22618234
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.
Asunto(s)

Texto completo: 1 Bases de datos: MEDLINE Asunto principal: Proteínas Bacterianas / Zinc / Cadmio / Ceruloplasmina Idioma: En Revista: Biochem Biophys Res Commun Año: 2012 Tipo del documento: Article País de afiliación: Japón

Texto completo: 1 Bases de datos: MEDLINE Asunto principal: Proteínas Bacterianas / Zinc / Cadmio / Ceruloplasmina Idioma: En Revista: Biochem Biophys Res Commun Año: 2012 Tipo del documento: Article País de afiliación: Japón