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Literature summary for 1.16.3.1 extracted from

  • 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 (2012), Biochem. Biophys. Res. Commun., 422, 745-750.
    View publication on PubMed

Crystallization (Commentary)

Crystallization (Comment) Organism
crystal structures of Zn2+- and Cd2+-bound forms of HP-NAP, and Cd2+-bound and apo forms of HP-NAP are determined: The coordination patterns of Zn2+ and Cd2+ are different but both metal ions can bind to the ferroxidase center (FOC), indicating that HP-NAP can store zinc and cadmium ions in addition to iron ions. Another zinc ion is found inside of the negatively-charged 3fold-related pore, as an iron ion in the iron-containing form, and therefore the pore is suitable for metal ions to pass through Helicobacter pylori

Metals/Ions

Metals/Ions Comment Organism Structure
Cd2+ crystal structures of Zn2+- and Cd2+-bound forms of HP-NAP, and Cd2+-bound and apo forms of HP-NAP are determined: The coordination patterns of Zn2+ and Cd2+ are different but both metal ions can bind to the ferroxidase center (FOC) Helicobacter pylori
Zn2+ crystal structures of Zn2+- and Cd2+-bound forms of HP-NAP, and Cd2+-bound and apo forms of HP-NAP are determined: The coordination patterns of Zn2+ and Cd2+ are different but both metal ions can bind to the ferroxidase center (FOC) Helicobacter pylori

Organism

Organism UniProt Comment Textmining
Helicobacter pylori G1UIZ2
-
-

Source Tissue

Source Tissue Comment Organism Textmining

Synonyms

Synonyms Comment Organism
HP-NAP
-
Helicobacter pylori
neutrophil-activating protein
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Helicobacter pylori