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

作者：Tsuruta Osamu; Yokoyama Hideshi^*; Fujii Satoshi

来源：Acta Crystallographica Section F-Structural Biology and Crystallization Communications, 2012, 68: 134-140.

DOI：10.1107/S1744309111052675

• Helicobacter pylori
• neutrophil-activating proteins
• ferroxidase centre
• solvent channels
• pores

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 angstrom resolution and an iron-loaded form (Fe-load) at 2.50 angstrom 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.

• 出版日期2012-2