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

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.

SUBMITTER: Kamada K

PROVIDER: S-EPMC30616 | biostudies-literature | 2001 Mar

REPOSITORIES: biostudies-literature

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

Kamada K K De Angelis J J Roeder R G RG Burley S K SK

Proceedings of the National Academy of Sciences of the United States of America 20010301 6

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 ...[more]

PMID: 11248041

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