2RNR

Solution structure of the complex between TFIIE alpha C-terminal acidic domain and TFIIH p62 PH domain

Summary for 2RNR

• Entry DOI: 10.2210/pdb2rnr/pdb
• Related: 1d8j 1d8k 1vd4 2RNQ
• Descriptor: Transcription initiation factor IIE subunit alpha, TFIIH basal transcription factor complex p62 subunit (2 entities in total)
• Functional Keywords: general transcription factor, human tfiie alpha, human tfiih p62, acidic domain, ph domain, dna damage, dna repair, transcription
• Biological source: Homo sapiens (human); More
• Cellular location: Nucleus: P29083 P32780
• Total number of polymer chains: 2
• Total formula weight: 19833.37

Authors

Okuda, M.,Nishimura, Y. (deposition date: 2008-01-31, release date: 2008-04-01, Last modification date: 2024-05-29)

Primary citation

Okuda, M.,Tanaka, A.,Satoh, M.,Mizuta, S.,Takazawa, M.,Ohkuma, Y.,Nishimura, Y.
Structural insight into the TFIIE-TFIIH interaction: TFIIE and p53 share the binding region on TFIIH
Embo J., 27:1161-1171, 2008

PubMed Abstract: RNA polymerase II and general transcription factors (GTFs) assemble on a promoter to form a transcription preinitiation complex (PIC). Among the GTFs, TFIIE recruits TFIIH to complete the PIC formation and regulates enzymatic activities of TFIIH. However, the mode of binding between TFIIE and TFIIH is poorly understood. Here, we demonstrate the specific binding of the C-terminal acidic domain (AC-D) of the human TFIIEalpha subunit to the pleckstrin homology domain (PH-D) of the human TFIIH p62 subunit and describe the solution structures of the free and PH-D-bound forms of AC-D. Although the flexible N-terminal acidic tail from AC-D wraps around PH-D, the core domain of AC-D also interacts with PH-D. AC-D employs an entirely novel binding mode, which differs from the amphipathic helix method used by many transcriptional activators. So the binding surface between PH-D and AC-D is much broader than the specific binding surface between PH-D and the p53 acidic fragments. From our in vitro studies, we demonstrate that this interaction could be a switch to replace p53 with TFIIE on TFIIH in transcription.

PubMed: 18354501
DOI: 10.1038/emboj.2008.47

Experimental method

SOLUTION NMR