3DOM

Crystal Structure of the complex between Tfb5 and the C-terminal domain of Tfb2

3DOM の概要

• エントリーDOI: 10.2210/pdb3dom/pdb
• 関連するPDBエントリー: 1YDL 2JNJ 3DGP
• 分子名称: RNA polymerase II transcription factor B subunit 2, RNA polymerase II transcription factor B subunit 5 (3 entities in total)
• 機能のキーワード: protein-protein complex, heterodimer, beta-alpha-beta split, beta-strand addition, dna damage, dna excision, dna repair, nucleus, transcription, transcription regulation
• 由来する生物種: Saccharomyces cerevisiae (yeast); 詳細
• 細胞内の位置: Nucleus : Q02939 Q3E7C1
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 41523.69

構造登録者

Kainov, D.E.,Cavarelli, J.,Egly, J.M.,Poterszman, A. (登録日: 2008-07-04, 公開日: 2008-08-19, 最終更新日: 2024-02-21)

主引用文献

Kainov, D.E.,Vitorino, M.,Cavarelli, J.,Poterszman, A.,Egly, J.M.
Structural basis for group A trichothiodystrophy
Nat.Struct.Mol.Biol., 15:980-984, 2008

PubMed Abstract: Patients with the rare neurodevelopmental repair syndrome known as group A trichothiodystrophy (TTD-A) carry mutations in the gene encoding the p8 subunit of the transcription and DNA repair factor TFIIH. Here we describe the crystal structure of a minimal complex between Tfb5, the yeast ortholog of p8, and the C-terminal domain of Tfb2, the yeast p52 subunit of TFIIH. The structure revealed that these two polypeptides adopt the same fold, forming a compact pseudosymmetric heterodimer via a beta-strand addition and coiled coils interactions between terminal alpha-helices. Furthermore, Tfb5 protects a hydrophobic surface in Tfb2 from solvent, providing a rationale for the influence of p8 in the stabilization of p52 and explaining why mutations that weaken p8-p52 interactions lead to a reduced intracellular TFIIH concentration and a defect in nucleotide-excision repair, a common feature of TTD cells.

PubMed: 19172752

実験手法

X-RAY DIFFRACTION (2.6 Å)