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Updated: May 25, 2026

One-step Negative Chromatographic Purification of Helicobacter pylori Neutrophil-activating Protein Overexpressed in Escherichia coli in Batch Mode
Published on: June 18, 2016
A new crystal lattice structure of Helicobacter pylori neutrophil-activating protein (HP-NAP)
Osamu Tsuruta1, Hideshi Yokoyama, Satoshi Fujii
1School of Pharmaceutical Sciences, University of Shizuoka, Suruga-ku, Shizuoka-shi, Shizuoka, Japan.
Abstract:
A new crystal lattice structure of Helicobacter pylori neutrophil-activating protein (HP-NAP) has been determined in two forms: the native state (Apo) at 2.20 Å resolution and an iron-loaded form (Fe-load) at 2.50 Å resolution. The highly solvated packing of the dodecameric shell is suitable for crystallographic study of the metal ion-uptake pathway. Like other bacterioferritins, HP-NAP forms a spherical dodecamer with 23 symmetry including two kinds of channels. Iron loading causes a series of conformational changes of amino-acid residues (Trp26, Asp52 and Glu56) at the ferroxidase centre.
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