1. Crystallization and preliminary X-ray diffraction analysis of an oxidized state of Ohr fromXylella fastidiosa
- Author
-
Francisco J. Medrano, João Alexandre Ribeiro Gonçalves Barbosa, José Renato Rosa Cussiol, Simone Vidigal Alves, Beatriz G. Guimarães, Luis Eduardo Soares Netto, and Marcos Antonio de Oliveira
- Subjects
Organic peroxide ,Protein Conformation ,Crystal structure ,Polyethylene Glycols ,law.invention ,Residue (chemistry) ,chemistry.chemical_compound ,Bacterial Proteins ,X-Ray Diffraction ,tert-Butylhydroperoxide ,Structural Biology ,law ,Proteobacteria ,Cysteine ,Crystallization ,Protein Structure, Quaternary ,Binding Sites ,biology ,Chemistry ,General Medicine ,biology.organism_classification ,Oxygen ,Crystallography ,X-ray crystallography ,Solvents ,biology.protein ,Protein quaternary structure ,Xylella fastidiosa ,Dimerization ,Peroxidase - 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 A using a synchrotron-radiation source. The crystal belongs to the hexagonal space group P6(5)22, with unit-cell parameters a = b = 87.66, c = 160.28 A. 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.
- Published
- 2004
- Full Text
- View/download PDF