2RNQ

Solution structure of the C-terminal acidic domain of TFIIE alpha

2RNQ の概要

• エントリーDOI: 10.2210/pdb2rnq/pdb
• 関連するPDBエントリー: 1d8j 1d8k 1vd4 2RNR
• 分子名称: Transcription initiation factor IIE subunit alpha (1 entity in total)
• 機能のキーワード: general transcription factor, human tfiie alpha, human tfiih p62, acidic domain, ph domain, transcription
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Nucleus: P29083
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 7382.92

構造登録者

Okuda, M.,Nishimura, Y. (登録日: 2008-01-31, 公開日: 2008-04-01, 最終更新日: 2024-05-29)

主引用文献

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

実験手法

SOLUTION NMR