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Literature DB >> 11248041

Crystal structure of the C-terminal domain of the RAP74 subunit of human transcription factor IIF.

K Kamada¹, J De Angelis, R G Roeder, S K Burley.

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.

Entities: Gene Species

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Year: 2001 PMID： 11248041 PMCID： PMC30616 DOI： 10.1073/pnas.051631098

Source DB: PubMed Journal: Proc Natl Acad Sci U S A ISSN： 0027-8424 Impact factor: 11.205

43 in total

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17 in total

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6. NMR structure of a complex containing the TFIIF subunit RAP74 and the RNA polymerase II carboxyl-terminal domain phosphatase FCP1.

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Journal: EMBO J Date: 2010-01-21 Impact factor: 11.598