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 interface that has trigonal bipyramidal geometry and is composed of two axial cysteines at 2.29(2) A, two equatorial histidines at 1.99(1) A, and a solvent-accessible coordination site. The final model for the Zn(II) site structure was determined by refining multiple-scattering extended X-ray absorption fine structure fits using the geometry predicted by homology modeling and ab initio calculations.

V. Martin-Diaconescu, M. Bellucci, F. Musiani, S. Ciurli, M. Maroney (2012). Unraveling the Helicobacter pylori UreG zinc binding site using X-ray absorption spectroscopy (XAS) and structural modeling. JBIC, 17, 353-361 [10.1007/s00775-011-0857-9].

Unraveling the Helicobacter pylori UreG zinc binding site using X-ray absorption spectroscopy (XAS) and structural modeling

BELLUCCI, MATTEO;MUSIANI, FRANCESCO;CIURLI, STEFANO LUCIANO;
2012

Abstract

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 interface that has trigonal bipyramidal geometry and is composed of two axial cysteines at 2.29(2) A, two equatorial histidines at 1.99(1) A, and a solvent-accessible coordination site. The final model for the Zn(II) site structure was determined by refining multiple-scattering extended X-ray absorption fine structure fits using the geometry predicted by homology modeling and ab initio calculations.
2012
V. Martin-Diaconescu, M. Bellucci, F. Musiani, S. Ciurli, M. Maroney (2012). Unraveling the Helicobacter pylori UreG zinc binding site using X-ray absorption spectroscopy (XAS) and structural modeling. JBIC, 17, 353-361 [10.1007/s00775-011-0857-9].
V. Martin-Diaconescu; M. Bellucci; F. Musiani; S. Ciurli; M. Maroney
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11585/117485
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