Referenced in: none

Automatically associated channels: TRP

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

Authors: Osamu Tsuruta, Hideshi Yokoyama, Satoshi Fujii

Journal, date & volume: Acta Crystallogr. Sect. F Struct. Biol. Cryst. Commun., 2012 Feb 1 , 68, 134-40

PubMed link: http://www.ncbi.nlm.nih.gov/pubmed/22297984

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.