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

Sung   Chul   Ha; Doo-Byoung      Oh; Kyeong   Kyu   Kim; Yang-Gyun      Kim

doi:10.2174/0929866053765608

Abstract

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: za motif, poxvirus, viral protein, z-dna, crystallization

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Protein & Peptide Letters

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

Volume: 12 Issue: 4

Author(s): Sung Chul Ha, Doo-Byoung Oh, Kyeong Kyu Kim and Yang-Gyun Kim

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

Abstract: 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.

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Ha Chul Sung, Oh Doo-Byoung, Kim Kyu Kyeong and Kim Yang-Gyun, Crystallization and Preliminary X-Ray Crystallographic Study of the Viral Zα Domain Bound to Left-Handed Z-DNA, Protein & Peptide Letters 2005; 12 (4) . https://dx.doi.org/10.2174/0929866053765608