1q1h

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(New page: 200px<br /><applet load="1q1h" size="450" color="white" frame="true" align="right" spinBox="true" caption="1q1h, resolution 2.90&Aring;" /> '''An extended winged h...)
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[[Image:1q1h.jpg|left|200px]]<br /><applet load="1q1h" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1q1h, resolution 2.90&Aring;" />
caption="1q1h, resolution 2.90&Aring;" />
'''An extended winged helix domain in general transcription factor E/IIE alpha'''<br />
'''An extended winged helix domain in general transcription factor E/IIE alpha'''<br />
==Overview==
==Overview==
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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.
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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==
==About this Structure==
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1Q1H is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sulfolobus_solfataricus Sulfolobus solfataricus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1Q1H OCA].
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1Q1H is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Sulfolobus_solfataricus Sulfolobus solfataricus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q1H OCA].
==Reference==
==Reference==
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[[Category: transcription initiation]]
[[Category: transcription initiation]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Sun Nov 25 03:24:17 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:34:49 2008''

Revision as of 12:34, 21 February 2008


1q1h, resolution 2.90Å

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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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