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Biomolecules 2014, 4(3), 600-615; doi:10.3390/biom4030600

Structures and Metal-Binding Properties of Helicobacter pylori Neutrophil-Activating Protein with a Di-Nuclear Ferroxidase Center

School of Pharmaceutical Sciences, University of Shizuoka, 52-1 Yada, Suruga-ku, Shizuoka 422-8526, Japan
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Received: 11 January 2014 / Revised: 3 June 2014 / Accepted: 4 June 2014 / Published: 26 June 2014
(This article belongs to the Special Issue Metal Binding Proteins)
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Abstract

Helicobacter pylori causes severe diseases, such as chronic gastritis, peptic ulcers, and stomach cancers. H. pylori neutrophil-activating protein (HP-NAP) is an iron storage protein that forms a dodecameric shell, promotes the adhesion of neutrophils to endothelial cells, and induces the production of reactive oxygen radicals. HP-NAP belongs to the DNA-protecting proteins under starved conditions (Dps) family, which has significant structural similarities to the dodecameric ferritin family. The crystal structures of the apo form and metal-ion bound forms, such as iron, zinc, and cadmium, of HP-NAP have been determined. This review focused on the structures and metal-binding properties of HP-NAP. These metal ions bind at the di-nuclear ferroxidase center (FOC) by different coordinating patterns. In comparison with the apo structure, metal loading causes a series of conformational changes in conserved residues among HP-NAP and Dps proteins (Trp26, Asp52, and Glu56) at the FOC. HP-NAP forms a spherical dodecamer with 23 symmetry including two kinds of pores. Metal ions have been identified around one of the pores; therefore, the negatively-charged pore is suitable for the passage of metal ions. View Full-Text
Keywords: Helicobacter pylori; neutrophil-activating protein; ferroxidase center; iron; zinc; cadmium; Dps; ferritin; solvent channel; pore Helicobacter pylori; neutrophil-activating protein; ferroxidase center; iron; zinc; cadmium; Dps; ferritin; solvent channel; pore
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This is an open access article distributed under the Creative Commons Attribution License (CC BY 3.0).

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Yokoyama, H.; Fujii, S. Structures and Metal-Binding Properties of Helicobacter pylori Neutrophil-Activating Protein with a Di-Nuclear Ferroxidase Center. Biomolecules 2014, 4, 600-615.

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