1Q1H

An extended winged helix domain in general transcription factor E/IIE alpha

Summary for 1Q1H

• Entry DOI: 10.2210/pdb1q1h/pdb
• Descriptor: Transcription Factor E (1 entity in total)
• Functional Keywords: tfe, tfiie, transcription initiation, preinitiation complex, rna polymerase ii, transcription bubble, promoter melting, tfiih, transcription
• Biological source: Sulfolobus solfataricus
• Total number of polymer chains: 1
• Total formula weight: 13091.11

Authors

Meinhart, A.,Blobel, J.,Cramer, P. (deposition date: 2003-07-21, release date: 2003-12-09, Last modification date: 2024-02-14)

Primary citation

Meinhart, A.,Blobel, J.,Cramer, P.
An Extended Winged Helix Domain in General Transcription Factor E/IIE alpha
J.Biol.Chem., 278:48267-48274, 2003

PubMed Abstract: 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.

PubMed: 13679366
DOI: 10.1074/jbc.M307874200

Experimental method

X-RAY DIFFRACTION (2.9 Å)