Functional disruption of HypB, a GTPase of Helicobacter pylori, by bismuth

Chem Commun (Camb). 2014 Feb 14;50(13):1611-4. doi: 10.1039/c3cc47644h.

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

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Anti-Bacterial Agents / pharmacology*
  • Bismuth / pharmacology*
  • GTP Phosphohydrolases / antagonists & inhibitors*
  • GTP Phosphohydrolases / metabolism
  • Helicobacter Infections / drug therapy
  • Helicobacter pylori / drug effects*
  • Helicobacter pylori / enzymology*
  • Humans
  • Models, Molecular
  • Protein Multimerization / drug effects*

Substances

  • Anti-Bacterial Agents
  • GTP Phosphohydrolases
  • Bismuth