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

Authors: de Oliveira, Marcos Antonio; Netto, Luis Eduardo Soares; Medrano, Francisco Javier; Barbosa, João Alexandre Ribeiro Gonçalves; Alves, Simone Vidigal; Cussiol, José Renato Rosa; Guimarães, Beatriz Gomes

Source: Acta Crystallographica Section D, Volume 60, Number 2, 1 February 2004 , pp. 337-339(3)

Publisher: Blackwell Publishing

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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 Å using a synchrotron-radiation source. The crystal belongs to the hexagonal space group P6₅22, with unit-cell parameters a = b = 87.66, c = 160.28 Å. 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.

Keywords: organic hydroperoxide-resistance protein (Ohr); Xylella fastidiosa; oxidized state

Document Type: Research article

DOI: 10.1107/S0907444903026799

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