4evb

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Crystal Structure HP-NAP from strain YS39 zinc soaked (20mM)Crystal Structure HP-NAP from strain YS39 zinc soaked (20mM)

Structural highlights

4evb 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

Helicobacter pylori neutrophil-activating protein (HP-NAP) is a Dps-like iron storage protein forming a dodecameric shell, and promotes adhesion of neutrophils to endothelial cells. The crystal structure of HP-NAP in a Zn(2+)- or Cd(2+)-bound form reveals the binding of two zinc or two cadmium ions and their bridged water molecule at the ferroxidase center (FOC). The two zinc ions are coordinated in a tetrahedral manner to the conserved residues among HP-NAP and Dps proteins. The two cadmium ions are coordinated in a trigonal-bipyramidal and distorted octahedral manner. In both structures, the second ion is more weakly coordinated than the first. Another zinc ion is found inside of the negatively-charged threefold-related pore, which is suitable for metal ions to pass through.

Crystal structure of Helicobacter pylori neutrophil-activating protein with a di-nuclear ferroxidase center in a zinc or cadmium-bound form.,Yokoyama H, Tsuruta O, Akao N, Fujii S Biochem Biophys Res Commun. 2012 Jun 15;422(4):745-50. Epub 2012 May 19. PMID:22618234[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

  1. Yokoyama H, Tsuruta O, Akao N, Fujii S. Crystal structure of Helicobacter pylori neutrophil-activating protein with a di-nuclear ferroxidase center in a zinc or cadmium-bound form. Biochem Biophys Res Commun. 2012 Jun 15;422(4):745-50. Epub 2012 May 19. PMID:22618234 doi:10.1016/j.bbrc.2012.05.073

4evb, resolution 2.50Å

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OCA