1WIJ

Solution Structure of the DNA-Binding Domain of Ethylene-Insensitive3-Like3

Summary for 1WIJ

• Entry DOI: 10.2210/pdb1wij/pdb
• Descriptor: ETHYLENE-INSENSITIVE3-like 3 protein (1 entity in total)
• Functional Keywords: dna-binding domain, structural genomics, riken structural genomics/proteomics initiative, rsgi, dna binding protein
• Biological source: Arabidopsis thaliana (thale cress)
• Cellular location: Nucleus (By similarity): O23116
• Total number of polymer chains: 1
• Total formula weight: 15645.97

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 citation

Yamasaki, K.,Kigawa, T.,Inoue, M.,Yamasaki, T.,Yabuki, T.,Aoki, M.,Seki, E.,Matsuda, T.,Tomo, Y.,Terada, T.,Shirouzu, M.,Tanaka, A.,Seki, M.,Shinozaki, K.,Yokoyama, S.
Solution structure of the major DNA-binding domain of Arabidopsis thaliana ethylene-insensitive3-like3.
J.Mol.Biol., 348:253-264, 2005

PubMed Abstract: Ethylene-insensitive3 (EIN3) and EIN3-like (EIL) proteins are essential transcription factors in the ethylene signaling of higher plants. The EIN3/EIL proteins bind to the promoter regions of the downstream genes and regulate their expression. The location of the DNA-binding domain (DBD) in the primary structure was unclear, since the proteins show no sequence similarity to other known DBDs. Here, we identify the major DBD of an EIN3/EIL protein, Arabidopsis thaliana EIL3, containing a key mutational site for DNA binding and signaling (ein3-3 site), and determine its solution structure by NMR spectroscopy. The structure consists of five alpha-helices, possessing a novel fold dissimilar to known DBD structures. By a chemical-shift perturbation analysis, a region including the ein3-3 site is suggested to be involved in DNA binding.

PubMed: 15811366
DOI: 10.1016/j.jmb.2005.02.065

Experimental method

SOLUTION NMR