1wij
From Proteopedia
(New page: 200px<br /><applet load="1wij" size="450" color="white" frame="true" align="right" spinBox="true" caption="1wij" /> '''Solution Structure of the DNA-Binding Domain...) |
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| - | [[Image:1wij.jpg|left|200px]]<br /><applet load="1wij" size=" | + | [[Image:1wij.jpg|left|200px]]<br /><applet load="1wij" size="350" color="white" frame="true" align="right" spinBox="true" |
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'''Solution Structure of the DNA-Binding Domain of Ethylene-Insensitive3-Like3'''<br /> | '''Solution Structure of the DNA-Binding Domain of Ethylene-Insensitive3-Like3'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Ethylene-insensitive3 (EIN3) and EIN3-like (EIL) proteins are essential | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1WIJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http:// | + | 1WIJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WIJ OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Inoue, M.]] | [[Category: Inoue, M.]] | ||
[[Category: Kigawa, T.]] | [[Category: Kigawa, T.]] | ||
| - | [[Category: RSGI, RIKEN | + | [[Category: RSGI, RIKEN Structural Genomics/Proteomics Initiative.]] |
[[Category: Yamasaki, K.]] | [[Category: Yamasaki, K.]] | ||
[[Category: Yokoyama, S.]] | [[Category: Yokoyama, S.]] | ||
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[[Category: structural genomics]] | [[Category: structural genomics]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:44:44 2008'' |
Revision as of 13:44, 21 February 2008
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Solution Structure of the DNA-Binding Domain of Ethylene-Insensitive3-Like3
Overview
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.
About this Structure
1WIJ is a Single protein structure of sequence from Arabidopsis thaliana. Full crystallographic information is available from OCA.
Reference
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
Page seeded by OCA on Thu Feb 21 15:44:44 2008
