Crystallization and preliminary X-ray diffraction analysis of an oxidized state of Ohr from Xylella fastidiosa

Autor(es)

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]

• Tipo de documento: Artigo Científico
• Fonte: ACTA CRYSTALLOGRAPHICA SECTION D-BIOLOGICAL CRYSTALLOGRAPHY; v. 60, n. 2, p. 337-339, Feb. 2004.
• Área do conhecimento: Ciências Biológicas - Bioquímica
• Assunto(s): Enzimas Peroxidase Difração por raios X Xylella fastidiosa

Resumo

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)

• Processo FAPESP: 01/07539-5 - Structural genomics program.
• Beneficiário: Luis Eduardo Soares Netto
• Modalidade de apoio: Auxílio à Pesquisa - Regular