1TAF

DROSOPHILA TBP ASSOCIATED FACTORS DTAFII42/DTAFII62 HETEROTETRAMER

Summary for 1TAF

• Entry DOI: 10.2210/pdb1taf/pdb
• Descriptor: TFIID TBP ASSOCIATED FACTOR 42, TFIID TBP ASSOCIATED FACTOR 62, ZINC ION, ... (4 entities in total)
• Functional Keywords: transcription initiation, histone fold, complex (two transcription factors)
• Biological source: Drosophila melanogaster (fruit fly); More
• Total number of polymer chains: 2
• Total formula weight: 15998.76

Authors

Xie, X.,Kokubo, T.,Cohen, S.L.,Mirza, U.A.,Hoffmann, A.,Chait, B.T.,Roeder, R.G.,Nakatani, Y.,Burley, S.K. (deposition date: 1996-06-01, release date: 1996-12-07, Last modification date: 2024-02-14)

Primary citation

Xie, X.,Kokubo, T.,Cohen, S.L.,Mirza, U.A.,Hoffmann, A.,Chait, B.T.,Roeder, R.G.,Nakatani, Y.,Burley, S.K.
Structural similarity between TAFs and the heterotetrameric core of the histone octamer.
Nature, 380:316-322, 1996

PubMed Abstract: 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.

PubMed: 8598927
DOI: 10.1038/380316a0

Experimental method

X-RAY DIFFRACTION (2 Å)