Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary 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)

EC Number Crystallization (Comment) Organism
1.16.3.1 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

EC Number Metals/Ions Comment Organism Structure
1.16.3.1 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
1.16.3.1 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

EC Number Organism UniProt Comment Textmining
1.16.3.1 Helicobacter pylori G1UIZ2
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining

Synonyms

EC Number Synonyms Comment Organism
1.16.3.1 HP-NAP
-
 Helicobacter pylori
1.16.3.1 neutrophil-activating protein
-
 Helicobacter pylori