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2LEX

Complex of the C-terminal WRKY domain of AtWRKY4 and a W-box DNA

Summary for 2LEX
Entry DOI10.2210/pdb2lex/pdb
NMR InformationBMRB: 17732
DescriptorProbable WRKY transcription factor 4, DNA (5'-D(*CP*G*CP*CP*TP*TP*TP*GP*AP*CP*CP*AP*GP*CP*GP*C)-3'), DNA (5'-D(*GP*CP*GP*C*TP*GP*GP*TP*CP*AP*AP*AP*GP*GP*CP*G)-3'), ... (4 entities in total)
Functional Keywordstranscription, transcription-dna complex, structural genomics, riken structural genomics/proteomics initiative, rsgi, transcription/dna
Biological sourceArabidopsis thaliana (thale-cress)
Cellular locationNucleus (Probable): Q9XI90
Total number of polymer chains3
Total formula weight18452.28
Authors
Yamasaki, K.,Kigawa, T.,Watanabe, S.,Inoue, M.,Yokoyama, S.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (deposition date: 2011-06-24, release date: 2012-01-18, Last modification date: 2024-05-01)
Primary citationYamasaki, K.,Kigawa, T.,Watanabe, S.,Inoue, M.,Yamasaki, T.,Seki, M.,Shinozaki, K.,Yokoyama, S.
Structural basis for sequence-spscific DNA recognition by an Arabidopsis WRKY transcription factor
J.Biol.Chem., 2012
Cited by
PubMed Abstract: The WRKY family transcription factors regulate plant-specific reactions that are mostly related to biotic and abiotic stresses. They share the WRKY domain, which recognizes a DNA element (TTGAC(C/T)) termed the W-box, in target genes. Here, we determined the solution structure of the C-terminal WRKY domain of Arabidopsis WRKY4 in complex with the W-box DNA by NMR. A four-stranded β-sheet enters the major groove of DNA in an atypical mode termed the β-wedge, where the sheet is nearly perpendicular to the DNA helical axis. Residues in the conserved WRKYGQK motif contact DNA bases mainly through extensive apolar contacts with thymine methyl groups. The importance of these contacts was verified by substituting the relevant T bases with U and by surface plasmon resonance analyses of DNA binding.
PubMed: 22219184
DOI: 10.1074/jbc.M111.279844
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

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