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

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.

SUBMITTER: Tsuruta O 

PROVIDER: S-EPMC3274388 | biostudies-literature | 2012 Feb

REPOSITORIES: biostudies-literature