Ontology highlight
ABSTRACT:
SUBMITTER: Martin-Diaconescu V
PROVIDER: S-EPMC3354701 | biostudies-literature | 2012 Mar
REPOSITORIES: biostudies-literature
Martin-Diaconescu Vlad V Bellucci Matteo M Musiani Francesco F Ciurli Stefano S Maroney Michael J MJ
Journal of biological inorganic chemistry : JBIC : a publication of the Society of Biological Inorganic Chemistry 20111109 3
The pathogenicity of Helicobacter pylori depends on the activity of urease for pH modification. Urease activity requires assembly of a dinickel active site that is facilitated in part by GTP hydrolysis by UreG. The proper functioning of Helicobacter pylori UreG (HpUreG) is dependent on Zn(II) binding and dimerization. X-ray absorption spectroscopy and structural modeling were used to elucidate the structure of the Zn(II) site in HpUreG. These studies independently indicated a site at the dimer i ...[more]