1J2X

Crystal structure of RAP74 C-terminal domain complexed with FCP1 C-terminal peptide

Summary for 1J2X

• Entry DOI: 10.2210/pdb1j2x/pdb
• Descriptor: Transcription initiation factor IIF, alpha subunit, RNA polymerase II CTD phosphatase, SULFATE ION, ... (5 entities in total)
• Functional Keywords: general transcription factor, rap74, rap30, tfiif, rna polymerase ii, winged-helix domain, fcp1, ctd, phosphatase, transcription
• Biological source: Homo sapiens (human); More
• Total number of polymer chains: 2
• Total formula weight: 10613.52

Authors

Kamada, K.,Roeder, R.G.,Burley, S.K. (deposition date: 2003-01-15, release date: 2003-01-30, Last modification date: 2023-10-25)

Primary citation

Kamada, K.,Roeder, R.G.,Burley, S.K.
Molecular mechanism of recruitment of TFIIF- associating RNA polymerase C-terminal domain phosphatase (FCP1) by transcription factor IIF
Proc.Natl.Acad.Sci.USA, 100:2296-2299, 2003

PubMed Abstract: After mRNA transcription termination in eukaryotes, the hyperphosphorylated form of RNA polymerase II (pol II0) must be recycled by TFIIF-associating C-terminal domain phosphatase (FCP1), the phosphatase responsible for dephosphorylating the C-terminal domain of the largest polymerase subunit. Transcription factor (TF)-IIF stimulates the activity of FCP1, and the RNA polymerase II-associating protein 74 subunit of TFIIF forms a complex with FCP1 in both human and yeast. Here, we report a cocrystal structure of the winged-helix domain of human RNA polymerase II-associating protein 74 bound to the alpha-helical C terminus of human FCP1 (residues 944-961). These results illustrate the molecular mechanism by which TFIIF efficiently recruits FCP1 to the pol II transcription machinery for recycling of the polymerase.

PubMed: 12591941
DOI: 10.1073/pnas.262798199

Experimental method

X-RAY DIFFRACTION (2 Å)