Abstract
Bismuth (Bi(3+)) binds equal molar amounts of HypB from Helicobacter pylori at the conserved metal site with a dissociation constant of 0.94 (±0.25) × 10(-17) μM, and concomitantly induces the protein dimerization similarly to Ni(2+). Excess Bi(3+) causes HypB further oligomerization, leading to HypB GTPase dysfunction. The results extend our understanding on the inhibitory mechanism of bismuth drugs against the pathogen.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Anti-Bacterial Agents / pharmacology*
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Bismuth / pharmacology*
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GTP Phosphohydrolases / antagonists & inhibitors*
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GTP Phosphohydrolases / metabolism
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Helicobacter Infections / drug therapy
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Helicobacter pylori / drug effects*
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Helicobacter pylori / enzymology*
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Humans
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Models, Molecular
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Protein Multimerization / drug effects*
Substances
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Anti-Bacterial Agents
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GTP Phosphohydrolases
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Bismuth