Journal
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
Volume 422, Issue 4, Pages 745-750Publisher
ACADEMIC PRESS INC ELSEVIER SCIENCE
DOI: 10.1016/j.bbrc.2012.05.073
Keywords
Helicobacter pylori; Neutrophil-activating protein; Zinc; Cadmium; Dps; Ferroxidase center
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Funding
- Japan Society for the Promotion of Science [22590039]
- Ministry of Education, Culture, Sports, Science and Technology in Japan [21770122]
- Grants-in-Aid for Scientific Research [21770122, 22590039] Funding Source: KAKEN
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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 Zn2+- or Cd2+-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. (C) 2012 Elsevier Inc. All rights reserved.
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