1vd4
From Proteopedia
(New page: 200px<br /> <applet load="1vd4" size="450" color="white" frame="true" align="right" spinBox="true" caption="1vd4" /> '''Solution structure of the zinc finger domai...) |
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'''Solution structure of the zinc finger domain of TFIIE alpha'''<br /> | '''Solution structure of the zinc finger domain of TFIIE alpha'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The zinc finger domain in the large subunit of TFIIE (TFIIEalpha) is | + | The zinc finger domain in the large subunit of TFIIE (TFIIEalpha) is phylogenetically conserved and is essential for transcription. Here, we determined the solution structure of this domain by using NMR. It consisted of one alpha-helix and five beta-strands, showing novel features distinct from previously determined zinc-binding structures. We created point mutants of TFIIEalpha in this domain and examined their binding abilities to other general transcription factors as well as their transcription activities. Four Zn(2+)-ligand mutants, in which each of cysteine residues at positions 129, 132, 154, and 157 was replaced by alanine, possessed no transcription activities on a linearized template, whereas, on a supercoiled template, interesting functional asymmetry was observed: although the C-terminal two mutants abolished transcription activity (<5%), the N-terminal two mutants retained about 20% activities. The N-terminal two mutants bound stronger to the small subunit of TFIIF than the wild type and the C-terminal two mutants were impaired in their binding abilities to the XPB subunits of TFIIH. These suggest that the structural integrity of the zinc finger domain is essential for the TFIIE function, particularly in the transition from the transcription initiation to elongation and the conformational tuning of this domain for appropriate positioning of TFIIF, TFIIH, and polymerase II would be needed depending on the situation and timing. |
==About this Structure== | ==About this Structure== | ||
| - | 1VD4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with ZN as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1VD4 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VD4 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: zinc finger]] | [[Category: zinc finger]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:34:02 2008'' |
Revision as of 13:34, 21 February 2008
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Solution structure of the zinc finger domain of TFIIE alpha
Overview
The zinc finger domain in the large subunit of TFIIE (TFIIEalpha) is phylogenetically conserved and is essential for transcription. Here, we determined the solution structure of this domain by using NMR. It consisted of one alpha-helix and five beta-strands, showing novel features distinct from previously determined zinc-binding structures. We created point mutants of TFIIEalpha in this domain and examined their binding abilities to other general transcription factors as well as their transcription activities. Four Zn(2+)-ligand mutants, in which each of cysteine residues at positions 129, 132, 154, and 157 was replaced by alanine, possessed no transcription activities on a linearized template, whereas, on a supercoiled template, interesting functional asymmetry was observed: although the C-terminal two mutants abolished transcription activity (<5%), the N-terminal two mutants retained about 20% activities. The N-terminal two mutants bound stronger to the small subunit of TFIIF than the wild type and the C-terminal two mutants were impaired in their binding abilities to the XPB subunits of TFIIH. These suggest that the structural integrity of the zinc finger domain is essential for the TFIIE function, particularly in the transition from the transcription initiation to elongation and the conformational tuning of this domain for appropriate positioning of TFIIF, TFIIH, and polymerase II would be needed depending on the situation and timing.
About this Structure
1VD4 is a Single protein structure of sequence from Homo sapiens with as ligand. Full crystallographic information is available from OCA.
Reference
A novel zinc finger structure in the large subunit of human general transcription factor TFIIE., Okuda M, Tanaka A, Arai Y, Satoh M, Okamura H, Nagadoi A, Hanaoka F, Ohkuma Y, Nishimura Y, J Biol Chem. 2004 Dec 3;279(49):51395-403. Epub 2004 Sep 22. PMID:15385556
Page seeded by OCA on Thu Feb 21 15:34:02 2008
Categories: Homo sapiens | Single protein | Arai, Y. | Hanaoka, F. | Nagadoi, A. | Nishimura, Y. | Ohkuma, Y. | Okamura, H. | Okuda, M. | Satoh, M. | Tanaka, A. | ZN | Zinc finger
