4EVB
Crystal Structure HP-NAP from strain YS39 zinc soaked (20mM)
Summary for 4EVB
Entry DOI | 10.2210/pdb4evb/pdb |
Related | 3T9J 3TA8 4EVC 4EVD 4EVE |
Descriptor | Neutrophil-activating protein, ZINC ION, 1,2-ETHANEDIOL, ... (5 entities in total) |
Functional Keywords | dodecamer, four-helix bundle, metal transport |
Biological source | Helicobacter pylori |
Total number of polymer chains | 1 |
Total formula weight | 19622.61 |
Authors | Yokoyama, H.,Tsuruta, O.,Akao, N.,Fujii, S. (deposition date: 2012-04-26, release date: 2012-06-27, Last modification date: 2023-11-08) |
Primary citation | 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., 422:745-750, 2012 Cited by PubMed Abstract: 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. PubMed: 22618234DOI: 10.1016/j.bbrc.2012.05.073 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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