1q1h
From Proteopedia
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An extended winged helix domain in general transcription factor E/IIE alpha
Overview
Initiation of eukaryotic mRNA transcription requires melting of promoter, DNA with the help of the general transcription factors TFIIE and TFIIH., Here we define a conserved and functionally essential N-terminal domain in, TFE, the archaeal homolog of the large TFIIE subunit alpha. X-ray, crystallography shows that this TFE domain adopts a winged, helix-turn-helix (winged helix) fold, extended by specific alpha-helices, at the N and C termini. Although the winged helix fold is often found in, DNA-binding proteins, we show that TFE is not a typical DNA-binding winged, helix protein, because its putative DNA-binding face shows a negatively, charged groove and an unusually long wing, and because the domain lacks, DNA-binding activity in vitro. The groove and a conserved hydrophobic, surface patch on the additional N-terminal alpha-helix may, however, allow, for interactions with other general transcription factors and RNA, polymerase. Homology modeling shows that the TFE domain is conserved in, TFIIE alpha, including the potential functional surfaces.
About this Structure
1Q1H is a Single protein structure of sequence from Sulfolobus solfataricus. Full crystallographic information is available from OCA.
Reference
An extended winged helix domain in general transcription factor E/IIE alpha., Meinhart A, Blobel J, Cramer P, J Biol Chem. 2003 Nov 28;278(48):48267-74. Epub 2003 Sep 17. PMID:13679366
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