1taf
From Proteopedia
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| - | [[Image:1taf.gif|left|200px]] | + | [[Image:1taf.gif|left|200px]] |
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| - | '''DROSOPHILA TBP ASSOCIATED FACTORS DTAFII42/DTAFII62 HETEROTETRAMER''' | + | {{Structure |
| + | |PDB= 1taf |SIZE=350|CAPTION= <scene name='initialview01'>1taf</scene>, resolution 2.0Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=ZN:ZINC ION'>ZN</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''DROSOPHILA TBP ASSOCIATED FACTORS DTAFII42/DTAFII62 HETEROTETRAMER''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1TAF is a [ | + | 1TAF is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Drosophila_melanogaster Drosophila melanogaster]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TAF OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/8598927 8598927] |
[[Category: Drosophila melanogaster]] | [[Category: Drosophila melanogaster]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: transcription initiation]] | [[Category: transcription initiation]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:16:01 2008'' |
Revision as of 12:16, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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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