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

Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 Feb 1;68(Pt 2):134-40. doi: 10.1107/S1744309111052675. Epub 2012 Jan 25.

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Bacterial Proteins / chemistry*
  • Crystallography, X-Ray
  • Helicobacter pylori / chemistry*
  • Models, Molecular
  • Protein Structure, Quaternary
  • Protein Structure, Tertiary
  • Structural Homology, Protein

Substances

  • Bacterial Proteins

Associated data

  • PDB/3T9J
  • PDB/3TA8