Crystal structure HP-NAP from strain YS39 iron loaded (cocrystallization 5mM)Crystal structure HP-NAP from strain YS39 iron loaded (cocrystallization 5mM)

Structural highlights

3ta8 is a 1 chain structure with sequence from Helicobacter pylori. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.5Å
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

G1UIZ3_HELPX

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

  1. 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

3ta8, resolution 2.50Å

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