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Crystallization and Preliminary X-Ray Crystallographic Study of the Viral Zα Domain Bound to Left-Handed Z-DNA

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The Zα domain (yabaZαE3L) of the E3L protein homologue from Yaba-like disease virus, a yatavirus, was cocrystallized with d(TCGCGCG)2 in the Z-conformation. The crystals belong to the P21212 space group, with unit-cell parameters a=51.20 Å, b=92.45 Å, c=48.02 Å, α=β= γ=90 . The diffraction data were collected up to a resolution of 2.2 Å. The structure of viral Za motif will provide an insight into how diverse Zα motifs recognize Z-DNA.

Keywords: crystallization; poxvirus; viral protein; z-dna; za motif

Document Type: Review Article


Affiliations: Department of Biochemistry, College of Medicine, Chung-Ang University, Seoul, 156-756, Korea.

Publication date: May 1, 2005

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  • Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.

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