| Full text | |
| Author(s): |
Soares Netto, L. E.
;
Medrano, F. J.
;
Ribeiro, J. A.
;
Barbosa, G.
;
Alves, S. V.
;
Cussiol, J. R. R.
;
Guimarães, B. G.
;
Oliveira, M. A. de
[8]
Total Authors: 8
|
| Document type: | Journal article |
| Source: | ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY; v. 60, n. 2, p. 337-339, Feb. 2004. |
| Field of knowledge: | Biological Sciences - Biochemistry |
| Abstract | |
Xylella fastidiosa organic hydroperoxide-resistance protein (Ohr) is a dithiol-dependent peroxidase that is widely conserved in several pathogenic bacteria with high affinity for organic hydroperoxides. The protein was crystallized using the hanging-drop vapour-diffusion method in the presence of PEG 4000 as precipitant after treatment with organic peroxide (t-butyl hydroperoxide). X-ray diffraction data were collected to a maximum resolution of 1.8 Angstrom using a synchrotronradiation source. The crystal belongs to the hexagonal space group P6(5)22, with unit-cell parameters a = b = 87.66, c = 160.28 Angstrom. The crystal structure was solved by molecular-replacement methods. The enzyme has a homodimeric quaternary structure similar to that observed for its homologue from Pseudomonas aeruginosa, but differs from the previous structure as the active-site residue Cys61 is oxidized. Structure refinement is in progress. (AU) | |