Structural highlights
Publication Abstract from PubMed
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 A resolution and an iron-loaded form (Fe-load) at 2.50 A 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.
A new crystal lattice structure of Helicobacter pylori neutrophil-activating protein (HP-NAP).,Tsuruta O, Yokoyama H, Fujii S Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 Feb 1;68(Pt 2):134-40., Epub 2012 Jan 25. PMID:22297984[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Tsuruta O, Yokoyama H, Fujii S. 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., Epub 2012 Jan 25. PMID:22297984 doi:10.1107/S1744309111052675
