Open AccessA new crystal lattice structure of Helicobacter pylori neutrophil‐activating protein (HP‐NAP)
Author(s) -
Tsuruta Osamu,
Yokoyama Hideshi,
Fujii Satoshi
Publication year - 2012
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309111052675
Subject(s) - dodecameric protein , crystallography , crystal structure , chemistry , helicobacter pylori , nap , metal , ion , biochemistry , dna , biology , organic chemistry , genetics , neuroscience
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.