3DGP

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

Summary for 3DGP

• Entry DOI: 10.2210/pdb3dgp/pdb
• Related: 1YDL 2JNJ
• Descriptor: RNA polymerase II transcription factor B subunit 2, RNA polymerase II transcription factor B subunit 5 (3 entities in total)
• Functional Keywords: protein-protein complex, beta-alpha-beta spilt, heterodimer, dna damage, dna excision, dna repair, nucleus, transcription, transcription regulation
• Biological source: Saccharomyces cerevisiae (Baker's yeast); More
• Cellular location: Nucleus (By similarity): Q02939; Nucleus: Q3E7C1
• Total number of polymer chains: 2
• Total formula weight: 17587.14

Authors

Kainov, D.E.,Cavarelli, J.,Egly, J.M.,Poterszman, A. (deposition date: 2008-06-14, release date: 2008-08-19, Last modification date: 2024-02-21)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.8 Å)