5GPY

Crystal structure of the human TFIIE complex

5GPY の概要

• エントリーDOI: 10.2210/pdb5gpy/pdb
• 分子名称: General transcription factor IIE subunit 1, Transcription initiation factor IIE subunit beta, ZINC ION, ... (4 entities in total)
• 機能のキーワード: general transcription factor, rna polymerase ii, transcription
• 由来する生物種: Homo sapiens (Human); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 38135.96

構造登録者

Obita, T.,Miwa, K.,Kojima, R.,Ohkuma, Y.,Tamura, Y.,Mizuguchi, M. (登録日: 2016-08-05, 公開日: 2016-11-02, 最終更新日: 2024-03-20)

主引用文献

Miwa, K.,Kojima, R.,Obita, T.,Ohkuma, Y.,Tamura, Y.,Mizuguchi, M.
Crystal Structure of Human General Transcription Factor TFIIE at Atomic Resolution
J.Mol.Biol., 428:4258-4266, 2016

PubMed Abstract: In eukaryotes, RNA polymerase II requires general transcription factors to initiate mRNA transcription. TFIIE subunits α and β form a heterodimer and recruit TFIIH to complete the assembly of the pre-initiation complex. Here, we have determined the crystal structure of human TFIIE at atomic resolution. The N-terminal half of TFIIEα forms an extended winged helix (WH) domain with an additional helix, followed by a zinc-finger domain. TFIIEβ contains the WH2 domain, followed by two coiled-coil helices intertwining with TFIIEα. We also showed that TFIIEα binds to TFIIEβ with nanomolar affinity using isothermal titration calorimetry. In addition, mutations on the residues involved in the interactions resulted in severe growth defects in yeast. Lack of the C-terminal region of yeast TFIIEβ causes a mild growth defect in vivo. These findings provide a structural basis for understanding the functional mechanisms of TFIIE in the context of pre-initiation complex formation and transcription initiation.

PubMed: 27639436
DOI: 10.1016/j.jmb.2016.09.008

実験手法

X-RAY DIFFRACTION (2.1 Å)