Crystallization and preliminary X-ray crystallographic study of the viral Zalpha domain bound to left-handed Z-DNA.
The Zalpha domain (yabaZalpha(E3L)) of the E3L protein homologue from Yaba-like disease virus, a yatavirus, was co-crystallized with d(TCGCGCG)(2) in the Z-conformation. The crystals belong to the P2(1)2(1)2 space group, with unit-cell parameters a=51.20 Angstroms, b=92.45 Angstroms, c=48.02 Angstroms, alpha=beta= gamma=90 degrees. The diffraction data were collected up to a resolution of 2.2 Angstroms. The structure of viral Zalpha motif will provide an insight into how diverse Zalpha motifs recognize Z-DNA.
Ha
Sung Chul
SC
Department of Molecular Cell Biology, Samsung Biomedical Research Institute, Sungkyunkwan University School of Medicine, Suwon, Korea.
Oh
Doo-Byoung
DB
Kim
Kyeong Kyu
KK
Kim
Yang-Gyun
YG
D003460:Crystallization; D018360:Crystallography, X-Ray; D043542:DNA, Z-Form / Q000737:chemistry*; D004268:DNA-Binding Proteins / Q000737:chemistry*; D017434:Protein Structure, Tertiary; D011994:Recombinant Proteins; D014764:Viral Proteins / Q000737:chemistry*; D014999:Yaba monkey tumor virus / Q000737:chemistry*
D043542:DNA, Z-Form; D004268:DNA-Binding Proteins; D011994:Recombinant Proteins; D014764:Viral Proteins