1vd4

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[[Image:1vd4.gif|left|200px]]
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{{Structure
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|GENE= GTF2E1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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|RELATEDENTRY=[[1d8j|1D8J]], [[1d8k|1D8K]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1vd4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vd4 OCA], [http://www.ebi.ac.uk/pdbsum/1vd4 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1vd4 RCSB]</span>
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'''Solution structure of the zinc finger domain of TFIIE alpha'''
'''Solution structure of the zinc finger domain of TFIIE alpha'''
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[[Category: Satoh, M.]]
[[Category: Satoh, M.]]
[[Category: Tanaka, A.]]
[[Category: Tanaka, A.]]
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[[Category: zinc finger]]
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[[Category: Zinc finger]]
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Revision as of 09:23, 3 May 2008

Template:STRUCTURE 1vd4

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. 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 Sat May 3 12:23:53 2008

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