Lee, Eun-Hae Seo, Yeo-Jin Ahn, Hee-Chul Kang, Young-Min Kim, Hee-Eun Lee, Yeon-Mi Choi, Byong-Seok Lee, Joon-Hwa 2024-01-20T18:04:42Z 2024-01-20T18:04:42Z 2021-09-05 2010-11-05 0014-5793 https://pubs.kist.re.kr/handle/201004/130929 The Yaba-like disease viruses (YLDV) are members of the Yatapoxvirus family and have double-stranded DNA genomes. The E3L protein, which is essential for pathogenesis in the vaccinia virus, consists of two domains: an N-terminal Z-DNA binding domain and a C-terminal RNA binding domain. The crystal structure of the E3L orthologue of YLDV (yabZ alpha(E3L)) bound to Z-DNA revealed that the overall structure of yabZ alpha(E3L) and its interaction with Z-DNA are very similar to those of hZ alpha(ADAR1). Here we have performed NMR hydrogen exchange experiments on the complexes between yabZ alpha(E3L) and d(CGCGCG)(2) with a variety of protein-to-DNA molar ratios. This study revealed that yabZ alpha(E3L) could efficiently change the B-form helix of the d(CGCGCG)(2) to left-handed Z-DNA via the active-mono B-Z transition pathway like hZ alpha(ADAR1). (C) 2010 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved. English WILEY HANDED Z-DNA CRYSTAL-STRUCTURE PROTON-EXCHANGE HUMAN ADAR1 BINDING VIRUS SEQUENCE KINETICS REVEALS COMPLEX NMR study of hydrogen exchange during the B-Z transition of a DNA duplex induced by the Z alpha domains of yatapoxvirus E3L Article 10.1016/j.febslet.2010.10.003 1 FEBS LETTERS, v.584, no.21, pp.4453 - 4457 FEBS LETTERS 584 21 4453 4457 scie scopus 000283573100014 2-s2.0-78049290009 Biochemistry & Molecular Biology Biophysics Cell Biology Biochemistry & Molecular Biology Biophysics Cell Biology Article HANDED Z-DNA CRYSTAL-STRUCTURE PROTON-EXCHANGE HUMAN ADAR1 BINDING VIRUS SEQUENCE KINETICS REVEALS COMPLEX NMR Z-DNA Hydrogen exchange Z-DNA binding protein E3L Poxvirus