1wij
From Proteopedia
Solution Structure of the DNA-Binding Domain of Ethylene-Insensitive3-Like3
Structural highlights
Function[EIL3_ARATH] Probable transcription factor that may be involved in the ethylene response pathway.[1] [2] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedEthylene-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. Solution structure of the major DNA-binding domain of Arabidopsis thaliana ethylene-insensitive3-like3.,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 J Mol Biol. 2005 Apr 29;348(2):253-64. PMID:15811366[3] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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