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

A new crystal lattice structure of Helicobacter pylori neutrophil‐activating protein (HP‐NAP) 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. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Acta Crystallographica Section F Wiley

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

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References (23)

Publisher
Wiley
Copyright
International Union of Crystallography, 2012
ISSN
1744-3091
eISSN
1744-3091
DOI
10.1107/S1744309111052675
pmid
22297984
Publisher site
See Article on Publisher Site

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.

Journal

Acta Crystallographica Section FWiley

Published: Feb 1, 2012

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