Purification, crystallization and preliminary diffraction studies of an ectromelia virus glutaredoxin
- Department of Medical Microbiology and Immunology, 1-15 Medical Sciences Building, University of Alberta, Edmonton, Alberta T6G 2H7 (Canada)
Ectromelia virus glutaredoxin has been crystallized in the presence of the reducing agent DTT. A diffraction data set has been collected and processed to 1.8 Å resolution. Ectromelia, vaccinia, smallpox and other closely related viruses of the orthopoxvirus genus encode a glutaredoxin gene that is not present in poxviruses outside of this genus. The vaccinia glutaredoxin O2L has been implicated as the reducing agent for ribonucleotide reductase and may thus play an important role in viral deoxyribonucleotide synthesis. As part of an effort to understand nucleotide metabolism by poxviruses, EVM053, the O2L ortholog of the ectromelia virus, has been crystallized. EVM053 crystallizes in space group C222{sub 1}, with unit-cell parameters a = 61.98, b = 67.57, c = 108.55 Å. Diffraction data have been processed to 1.8 Å resolution and a self-rotation function indicates that there are two molecules per asymmetric unit.
- OSTI ID:
- 22356030
- Journal Information:
- Acta Crystallographica. Section F, Vol. 61, Issue Pt 6; Other Information: PMCID: PMC1952336; PMID: 16511093; PUBLISHER-ID: mp5002; OAI: oai:pubmedcentral.nih.gov:1952336; Copyright (c) International Union of Crystallography 2005; Country of input: International Atomic Energy Agency (IAEA); ISSN 1744-3091
- Country of Publication:
- United Kingdom
- Language:
- English
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