Solution Structure of an Arabidopsis WRKY DNA Binding Domainw⃞
Solution Structure of an Arabidopsis WRKY DNA Binding Domainw⃞
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DOI:
10.1105/tpc.104.026435
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发表时间:
2005-03
期刊:
影响因子:
--
通讯作者:
K. Yamasaki;T. Kigawa;M. Inoue;M. Tateno;T. Yamasaki;T. Yabuki;M. Aoki;Eiko Seki;T. Matsuda
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文献类型:
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作者:
K. Yamasaki;T. Kigawa;M. Inoue;M. Tateno;T. Yamasaki;T. Yabuki;M. Aoki;Eiko Seki;T. Matsuda
The WRKY proteins comprise a major family of transcription factors that are essential in pathogen and salicylic acid responses of higher plants as well as a variety of plant-specific reactions. They share a DNA binding domain, designated as the WRKY domain, which contains an invariant WRKYGQK sequence and a CX4–5CX22–23HXH zinc binding motif. Herein, we report the NMR solution structure of the C-terminal WRKY domain of the Arabidopsis thaliana WRKY4 protein. The structure consists of a four-stranded β-sheet, with a zinc binding pocket formed by the conserved Cys/His residues located at one end of the β-sheet, revealing a novel zinc and DNA binding structure. The WRKYGQK residues correspond to the most N-terminal β-strand, kinked in the middle of the sequence by the Gly residue, which enables extensive hydrophobic interactions involving the Trp residue and contributes to the structural stability of the β-sheet. Based on a profile of NMR chemical shift perturbations, we propose that the same strand enters the DNA groove and forms contacts with the DNA bases.