Literature DB >> 22297984

A new crystal lattice structure of Helicobacter pylori neutrophil-activating protein (HP-NAP).

Osamu Tsuruta1, Hideshi Yokoyama, Satoshi Fujii.   

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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Year:  2012        PMID： 22297984      PMCID： PMC3274388          DOI： 10.1107/S1744309111052675

Source DB:  PubMed          Journal:  Acta Crystallogr Sect F Struct Biol Cryst Commun        ISSN： 1744-3091


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