5NUS

Structure of a minimal complex between p44 and p34 from Chaetomium thermophilum

5NUS の概要

• エントリーDOI: 10.2210/pdb5nus/pdb
• 分子名称: p34, p44, ZINC ION, ... (4 entities in total)
• 機能のキーワード: ring finger domain, von willebrand factor a like, transcription
• 由来する生物種: Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 44367.60

構造登録者

Koelmel, W.,Schoenwetter, E.,Kuper, J.,Schmitt, D.R.,Kisker, C. (登録日: 2017-05-02, 公開日: 2017-10-18, 最終更新日: 2024-05-08)

主引用文献

Radu, L.,Schoenwetter, E.,Braun, C.,Marcoux, J.,Koelmel, W.,Schmitt, D.R.,Kuper, J.,Cianferani, S.,Egly, J.M.,Poterszman, A.,Kisker, C.
The intricate network between the p34 and p44 subunits is central to the activity of the transcription/DNA repair factor TFIIH.
Nucleic Acids Res., 45:10872-10883, 2017

PubMed Abstract: The general transcription factor IIH (TFIIH) is a multi-protein complex and its 10 subunits are engaged in an intricate protein-protein interaction network critical for the regulation of its transcription and DNA repair activities that are so far little understood on a molecular level. In this study, we focused on the p44 and the p34 subunits, which are central for the structural integrity of core-TFIIH. We solved crystal structures of a complex formed by the p34 N-terminal vWA and p44 C-terminal zinc binding domains from Chaetomium thermophilum and from Homo sapiens. Intriguingly, our functional analyses clearly revealed the presence of a second interface located in the C-terminal zinc binding region of p34, which can rescue a disrupted interaction between the p34 vWA and the p44 RING domain. In addition, we demonstrate that the C-terminal zinc binding domain of p34 assumes a central role with respect to the stability and function of TFIIH. Our data reveal a redundant interaction network within core-TFIIH, which may serve to minimize the susceptibility to mutational impairment. This provides first insights why so far no mutations in the p34 or p44 TFIIH-core subunits have been identified that would lead to the hallmark nucleotide excision repair syndromes xeroderma pigmentosum or trichothiodystrophy.

PubMed: 28977422
DOI: 10.1093/nar/gkx743

実験手法

X-RAY DIFFRACTION (2.2 Å)