1I27

CRYSTAL STRUCTURE OF THE C-TERMINAL DOMAIN OF THE RAP74 SUBUNIT OF HUMAN TRANSCRIPTION FACTOR IIF (TFIIF)

Summary for 1I27

• Entry DOI: 10.2210/pdb1i27/pdb
• Descriptor: TRANSCRIPTION FACTOR IIF, ZINC ION (3 entities in total)
• Functional Keywords: general transcription factor, rap74, rap30, tfiif, rna polymerase ii, winged-helix domain, transcription
• Biological source: Homo sapiens (human)
• Total number of polymer chains: 1
• Total formula weight: 8440.21

Authors

Kamada, K.,De Angelis, J.,Roeder, R.G.,Burley, S.K. (deposition date: 2001-02-07, release date: 2001-03-07, Last modification date: 2024-02-07)

Primary citation

Kamada, K.,De Angelis, J.,Roeder, R.G.,Burley, S.K.
Crystal structure of the C-terminal domain of the RAP74 subunit of human transcription factor IIF.
Proc.Natl.Acad.Sci.USA, 98:3115-3120, 2001

PubMed Abstract: The x-ray structure of a C-terminal fragment of the RAP74 subunit of human transcription factor (TF) IIF has been determined at 1.02-A resolution. The alpha/beta structure is strikingly similar to the globular domain of linker histone H5 and the DNA-binding domain of hepatocyte nuclear factor 3gamma (HNF-3gamma), making it a winged-helix protein. The surface electrostatic properties of this compact domain differ significantly from those of bona fide winged-helix transcription factors (HNF-3gamma and RFX1) and from the winged-helix domains found within the RAP30 subunit of TFIIF and the beta subunit of TFIIE. RAP74 has been shown to interact with the TFIIF-associated C-terminal domain phosphatase FCP1, and a putative phosphatase binding site has been identified within the RAP74 winged-helix domain.

PubMed: 11248041
DOI: 10.1073/pnas.051631098

Experimental method

X-RAY DIFFRACTION (1.02 Å)