1taf

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1taf, resolution 2.0Å

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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 ZN 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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