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Acta Crystallogr Sect F Struct Biol Cryst Commun. 2012 Dec 1;68(Pt 12):1557-9. doi: 10.1107/S174430911204657X. Epub 2012 Nov 28.

Preliminary crystallographic analysis of the Megavirus superoxide dismutase.

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1
Information Génomique et Structurale, IGS UMR7256, CNRS, Aix-Marseille Université, IMM, FR3479, 163 Avenue de Luminy-case 934, 13288 Marseille CEDEX 09, France.

Abstract

Megavirus chilensis, a close relative of the Mimivirus giant virus, is able to replicate in Acanthamoeba castellanii. The first step of viral infection involves the internalization of the virions in host vacuoles. It has been experimentally demonstrated that Mimivirus particles contain many proteins capable of resisting oxidative stress, as encountered in the phagocytic process. These proteins are conserved in Megavirus, which has an additional gene (Mg277) encoding a putative superoxide dismutase. The Mg277 ORF product was overexpressed in Escherichia coli, purified and crystallized. A SAD data set was collected to 2.24 Å resolution at the selenium peak wavelength on the BM30 beamline at the ESRF from a single crystal of selenomethionine-substituted recombinant superoxide dismutase protein.

PMID:
23192047
PMCID:
PMC3509988
DOI:
10.1107/S174430911204657X
[Indexed for MEDLINE]
Free PMC Article
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