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1WJ2

Solution Structure of the C-terminal WRKY Domain of AtWRKY4

Summary for 1WJ2
Entry DOI10.2210/pdb1wj2/pdb
DescriptorProbable WRKY transcription factor 4, ZINC ION (2 entities in total)
Functional Keywordsdna-binding domain, zinc-binding, structural genomics, riken structural genomics/proteomics initiative, rsgi, dna binding protein
Biological sourceArabidopsis thaliana (thale cress)
Cellular locationNucleus (Probable): Q9XI90
Total number of polymer chains1
Total formula weight8652.94
Authors
Yamasaki, K.,Inoue, M.,Kigawa, T.,Yokoyama, S.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (deposition date: 2004-05-28, release date: 2004-11-28, Last modification date: 2024-05-29)
Primary citationYamasaki, K.,Kigawa, T.,Inoue, M.,Tateno, M.,Yamasaki, T.,Yabuki, T.,Aoki, M.,Seki, E.,Matsuda, T.,Tomo, Y.,Hayami, N.,Terada, T.,Shirouzu, M.,Tanaka, A.,Seki, M.,Shinozaki, K.,Yokoyama, S.
Solution structure of an Arabidopsis WRKY DNA binding domain.
Plant Cell, 17:944-956, 2005
Cited by
PubMed Abstract: 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 beta-sheet, with a zinc binding pocket formed by the conserved Cys/His residues located at one end of the beta-sheet, revealing a novel zinc and DNA binding structure. The WRKYGQK residues correspond to the most N-terminal beta-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 beta-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.
PubMed: 15705956
DOI: 10.1105/tpc.104.026435
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

237735

数据于2025-06-18公开中

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