4EVE: Crystal Structure Hp-Nap From Strain Ys29 In Apo Form

Citation:
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.
PDB ID: 4EVEDownload
MMDB ID: 100909
PDB Deposition Date: 2012/4/26
Updated in MMDB: 2012/06
Experimental Method:
x-ray diffraction
Resolution: 2.1  Å
Source Organism:
Similar Structures:
Biological Unit for 4EVE: dodecameric; determined by author and by software (PISA)
Molecular Components in 4EVE
Label Count Molecule
Proteins (12 molecules)
12
Neutrophil-activating Protein
Molecule annotation
Chemicals (23 molecules)
1
23
* Click molecule labels to explore molecular sequence information.

Citing MMDB
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