A new crystal lattice structure ofHelicobacter pylorineutrophil-activating protein (HP-NAP)
Copyright policy )A new crystal lattice structure ofHelicobacter pylorineutrophil-activating protein (HP-NAP)
A new crystal lattice structure ofHelicobacter pylorineutrophil-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.
- University of Shizuoka Japan
- University of Shizuoka Japan
Models, Molecular, Bacterial Proteins, Helicobacter pylori, Structural Homology, Protein, Crystallography, X-Ray, Protein Structure, Quaternary, Protein Structure, Tertiary
Models, Molecular, Bacterial Proteins, Helicobacter pylori, Structural Homology, Protein, Crystallography, X-Ray, Protein Structure, Quaternary, Protein Structure, Tertiary
selected citations These citations are derived from selected sources.This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).11 popularity This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network.Average influence This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).Average impulse This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network.Average
Citations provided by BIP!Popularity provided by BIP!