title: Functional disruption of HypB, a GTPase of Helicobacter pylori, by bismuth.
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.
authors.affiliation: Department of Chemistry, The University of Hong Kong, Pokfulam Road, Hong Kong, P. R. China. hsun@hku.hk.
authors.forename: Wei
authors.initials: W
authors.lastname: Xia
authors.forename: Hongyan
authors.initials: H
authors.lastname: Li
authors.forename: Hongzhe
authors.initials: H
authors.lastname: Sun
mesh_terms: D000900:Anti-Bacterial Agents / Q000494:pharmacology*; D001729:Bismuth / Q000494:pharmacology*; D020558:GTP Phosphohydrolases / Q000037:antagonists & inhibitors* / Q000378:metabolism; D016481:Helicobacter Infections / Q000188:drug therapy; D016480:Helicobacter pylori / Q000187:drug effects* / Q000201:enzymology*; D006801:Humans; D008958:Models, Molecular; D055503:Protein Multimerization / Q000187:drug effects*
chemical_list: D000900:Anti-Bacterial Agents; D020558:GTP Phosphohydrolases; D001729:Bismuth