1taf

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(New page: 200px<br /><applet load="1taf" size="450" color="white" frame="true" align="right" spinBox="true" caption="1taf, resolution 2.0&Aring;" /> '''DROSOPHILA TBP ASSOCI...)
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[[Image:1taf.gif|left|200px]]<br /><applet load="1taf" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1taf.gif|left|200px]]<br /><applet load="1taf" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1taf, resolution 2.0&Aring;" />
caption="1taf, resolution 2.0&Aring;" />
'''DROSOPHILA TBP ASSOCIATED FACTORS DTAFII42/DTAFII62 HETEROTETRAMER'''<br />
'''DROSOPHILA TBP ASSOCIATED FACTORS DTAFII42/DTAFII62 HETEROTETRAMER'''<br />
==Overview==
==Overview==
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A complex of two TFIID TATA box-binding protein-associated factors (TA, FIIs) is described at 2.0A resolution. The amino-terminal portions of, dTAFII42 and dTAFII62 from Drosophila adopt the canonical histone fold, consisting of two short alpha-helices flanking a long central alpha-helix., Like histones H3 and H4, dTAFII42 and dTAFII62 form an intimate, heterodimer by extensive hydrophobic contacts between the paired, molecules. In solution and in the crystalline state, the dTAFII42/dTAFII62, complex exists as a heterotetramer, resembling the (H3/H4)2, heterotetrameric core of the histone octamer, suggesting that TFIID, contains a histone octamer-like substructure.
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A complex of two TFIID TATA box-binding protein-associated factors (TA FIIs) is described at 2.0A resolution. The amino-terminal portions of dTAFII42 and dTAFII62 from Drosophila adopt the canonical histone fold, consisting of two short alpha-helices flanking a long central alpha-helix. Like histones H3 and H4, dTAFII42 and dTAFII62 form an intimate heterodimer by extensive hydrophobic contacts between the paired molecules. In solution and in the crystalline state, the dTAFII42/dTAFII62 complex exists as a heterotetramer, resembling the (H3/H4)2 heterotetrameric core of the histone octamer, suggesting that TFIID contains a histone octamer-like substructure.
==About this Structure==
==About this Structure==
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1TAF is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster] with ZN as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1TAF OCA].
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1TAF is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster] 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=1TAF OCA].
==Reference==
==Reference==
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[[Category: Drosophila melanogaster]]
[[Category: Drosophila melanogaster]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: Burley, S.K.]]
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[[Category: Burley, S K.]]
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[[Category: Chait, B.T.]]
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[[Category: Chait, B T.]]
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[[Category: Cohen, S.L.]]
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[[Category: Cohen, S L.]]
[[Category: Hoffmann, A.]]
[[Category: Hoffmann, A.]]
[[Category: Kokubo, T.]]
[[Category: Kokubo, T.]]
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[[Category: Mirza, U.A.]]
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[[Category: Mirza, U A.]]
[[Category: Nakatani, Y.]]
[[Category: Nakatani, Y.]]
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[[Category: Roeder, R.G.]]
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[[Category: Roeder, R G.]]
[[Category: Xie, X.]]
[[Category: Xie, X.]]
[[Category: ZN]]
[[Category: ZN]]
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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 Wed Nov 21 03:07:01 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:11:38 2008''

Revision as of 13:11, 21 February 2008


1taf, resolution 2.0Å

Drag the structure with the mouse to rotate

DROSOPHILA TBP ASSOCIATED FACTORS DTAFII42/DTAFII62 HETEROTETRAMER

Overview

A complex of two TFIID TATA box-binding protein-associated factors (TA FIIs) is described at 2.0A resolution. The amino-terminal portions of dTAFII42 and dTAFII62 from Drosophila adopt the canonical histone fold, consisting of two short alpha-helices flanking a long central alpha-helix. Like histones H3 and H4, dTAFII42 and dTAFII62 form an intimate heterodimer by extensive hydrophobic contacts between the paired molecules. In solution and in the crystalline state, the dTAFII42/dTAFII62 complex exists as a heterotetramer, resembling the (H3/H4)2 heterotetrameric core of the histone octamer, suggesting that TFIID contains a histone octamer-like substructure.

About this Structure

1TAF is a Protein complex structure of sequences from Drosophila melanogaster with as ligand. Full crystallographic information is available from OCA.

Reference

Structural similarity between TAFs and the heterotetrameric core of the histone octamer., Xie X, Kokubo T, Cohen SL, Mirza UA, Hoffmann A, Chait BT, Roeder RG, Nakatani Y, Burley SK, Nature. 1996 Mar 28;380(6572):316-22. PMID:8598927

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