Papers by Anthony ZOROPOGUI
Journal of …, Jan 1, 2012
The pathogenic strain Nocardia cyriacigeorgica GUH-2 was isolated from a fatal human nocardiosis ... more The pathogenic strain Nocardia cyriacigeorgica GUH-2 was isolated from a fatal human nocardiosis case, and its genome was sequenced. The complete genomic sequence of this strain contains 6,194,645 bp, an average G؉C content of 68.37%, and no plasmids. We also identified several protein-coding genes to which N. cyriacigeorgica's virulence can potentially be attributed.
… Section F: Structural …, Jan 1, 2007
CzcE is encoded by the czc determinant that allows Cupriavidus metallidurans CH34 to modulate its... more CzcE is encoded by the czc determinant that allows Cupriavidus metallidurans CH34 to modulate its internal concentrations of cobalt, zinc and cadmium. This periplasmic protein was overproduced in its mature form in Escherichia coli and purified in two steps. After preliminary screening of crystallization conditions using a robot, well diffracting crystals were obtained using the hanging-drop vapour-diffusion method. Crystals diffracted to 1.96 Å using synchrotron radiation. They belonged to the monoclinic space group C2, with unit-cell parameters a = 105.54, b = 29.68, c = 71.10 Å . The asymmetric unit is expected to contain a dimer, in agreement with the quaternary structure deduced from gelfiltration experiments.
Biochemical and biophysical …, Jan 1, 2008
CzcE is encoded by the most distal gene of the czc determinant that allows Cupriavidus metallidur... more CzcE is encoded by the most distal gene of the czc determinant that allows Cupriavidus metallidurans CH34 to modulate its internal concentrations of cobalt, zinc and cadmium by regulation of the expression of the efflux pump CzcCBA. We have overproduced and purified CzcE. CzcE is a periplasm-located dimeric protein able to bind specifically 4 Cu-equivalent per dimer. Spectrophotometry and EPR are indicative of type II copper with typical d–d transitions. Re-oxidation of fully reduced CzcE led to the formation of an air stable semi-reduced form binding both 2 Cu(I) and 2 Cu(II) ions. The spectroscopic characteristics of the semi-reduced form are different of those of the oxidized one, suggesting a change in the environment of Cu(II).
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Papers by Anthony ZOROPOGUI