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.
School of Pharmaceutical Sciences, University of Shizuoka, Suruga-ku, Shizuoka-shi, Shizuoka, Japan.
Osamu
O
Tsuruta
Hideshi
H
Yokoyama
Satoshi
S
Fujii
D001426:Bacterial Proteins / Q000737:chemistry*; D018360:Crystallography, X-Ray; D016480:Helicobacter pylori / Q000737:chemistry*; D008958:Models, Molecular; D020836:Protein Structure, Quaternary; D017434:Protein Structure, Tertiary; D040681:Structural Homology, Protein
D001426:Bacterial Proteins