Crystal structure of the C-terminal domain of the RAP74 subunit of human transcription factor IIF
- 13 March 2001
- journal article
- Published by Proceedings of the National Academy of Sciences in Proceedings of the National Academy of Sciences
- Vol. 98 (6) , 3115-3120
- https://doi.org/10.1073/pnas.051631098
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-Å resolution. The α/β structure is strikingly similar to the globular domain of linker histone H5 and the DNA-binding domain of hepatocyte nuclear factor 3γ (HNF-3γ), 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-3γ and RFX1) and from the winged-helix domains found within the RAP30 subunit of TFIIF and the β 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.Keywords
This publication has 49 references indexed in Scilit:
- Novel dimerization fold of RAP30/RAP74 in human TFIIF at 1.7 Å resolution 1 1Edited by K. NagaiJournal of Molecular Biology, 2000
- Reconstitution of the Transcription Factor TFIIHMolecular Cell, 1999
- Crystal structure of the cyanobacterial metallothionein repressor SmtB: a model for metalloregulatory proteins 1 1Edited by D. ReesJournal of Molecular Biology, 1998
- [20] Processing of X-ray diffraction data collected in oscillation modePublished by Elsevier ,1997
- Purification and Characterization of an RNA Polymerase II Phosphatase from YeastJournal of Biological Chemistry, 1996
- RNA Polymerase II-associated Protein (RAP) 74 Binds Transcription Factor (TF) IIB and Blocks TFIIB-RAP30 BindingPublished by Elsevier ,1996
- Localization of Subunits of Transcription Factors IIE and IIF Immediately Upstream of the Transcriptional Initiation Site of the Adenovirus Major Late PromoterPublished by Elsevier ,1996
- Probing the solution structure of the DNA‐binding protein Max by a combination of proteolysis and mass spectrometryProtein Science, 1995
- The CCP4 suite: programs for protein crystallographyActa Crystallographica Section D-Biological Crystallography, 1994
- GENERAL INITIATION FACTORS FOR RNA POLYMERASE IIAnnual Review of Biochemistry, 1993