1EQF

CRYSTAL STRUCTURE OF THE DOUBLE BROMODOMAIN MODULE FROM HUMAN TAFII250

Summary for 1EQF

• Entry DOI: 10.2210/pdb1eqf/pdb
• Descriptor: RNA POLYMERASE II TRANSCRIPTION INITIATION FACTOR, SULFATE ION (3 entities in total)
• Functional Keywords: four-helix bundle, acetylated histone-tail binding protein, transcription
• Biological source: Homo sapiens (human)
• Cellular location: Nucleus: P21675
• Total number of polymer chains: 1
• Total formula weight: 32802.28

Authors

Jacobson, R.H.,Ladurner, A.G.,King, D.S.,Tjian, R. (deposition date: 2000-04-04, release date: 2000-06-07, Last modification date: 2011-07-13)

Primary citation

Jacobson, R.H.,Ladurner, A.G.,King, D.S.,Tjian, R.
Structure and function of a human TAFII250 double bromodomain module.
Science, 288:1422-1425, 2000

PubMed Abstract: TFIID is a large multiprotein complex that initiates assembly of the transcription machinery. It is unclear how TFIID recognizes promoters in vivo when templates are nucleosome-bound. Here, it is shown that TAFII250, the largest subunit of TFIID, contains two tandem bromodomain modules that bind selectively to multiply acetylated histone H4 peptides. The 2.1 angstrom crystal structure of the double bromodomain reveals two side-by-side, four-helix bundles with a highly polarized surface charge distribution. Each bundle contains an Nepsilon-acetyllysine binding pocket at its center, which results in a structure ideally suited for recognition of diacetylated histone H4 tails. Thus, TFIID may be targeted to specific chromatin-bound promoters and may play a role in chromatin recognition.

PubMed: 10827952
DOI: 10.1126/science.288.5470.1422

Experimental method

X-RAY DIFFRACTION (2.1 Å)