4PN7

Crystal Structure of the TFIIH p34 N-terminal Domain

4PN7 の概要

• エントリーDOI: 10.2210/pdb4pn7/pdb
• 分子名称: Putative transcription factor (2 entities in total)
• 機能のキーワード: vwa domain, transcription
• 由来する生物種: Chaetomium thermophilum
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 31972.96

構造登録者

Schmitt, D.R.,Kuper, J.,Elias, A.,Kisker, C. (登録日: 2014-05-23, 公開日: 2014-07-23, 最終更新日: 2023-12-27)

主引用文献

Schmitt, D.R.,Kuper, J.,Elias, A.,Kisker, C.
The Structure of the TFIIH p34 Subunit Reveals a Von Willebrand Factor A Like Fold.
Plos One, 9:e102389-e102389, 2014

PubMed Abstract: RNA polymerase II dependent transcription and nucleotide excision repair are mediated by a multifaceted interplay of subunits within the general transcription factor II H (TFIIH). A better understanding of the molecular structure of TFIIH is the key to unravel the mechanism of action of this versatile protein complex within these vital cellular processes. The importance of this complex becomes further evident in the context of severe diseases like xeroderma pigmentosum, Cockayne's syndrome and trichothiodystrophy, that arise from single point mutations in TFIIH subunits. Here we describe the structure of the p34 subunit of the TFIIH complex from the eukaryotic thermophilic fungus Chaetomium thermophilum. The structure revealed that p34 contains a von Willebrand Factor A (vWA) like domain, a fold which is generally known to be involved in protein-protein interactions. Within TFIIH p34 strongly interacts with p44, a positive regulator of the helicase XPD. Putative protein-protein interfaces are analyzed and possible binding sites for the p34-p44 interaction suggested.

PubMed: 25013903
DOI: 10.1371/journal.pone.0102389

実験手法

X-RAY DIFFRACTION (2.801 Å)