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5O85

p34-p44 complex

Summary for 5O85
Entry DOI10.2210/pdb5o85/pdb
DescriptorGeneral transcription factor IIH subunit 3, General transcription factor IIH subunit 2, ZINC ION (3 entities in total)
Functional Keywordsdna repair, tfiih, tfiih interaction network, p34-p44 complex, transcription
Biological sourceHomo sapiens (Human)
More
Total number of polymer chains4
Total formula weight158025.52
Authors
Radu, L.,Poterszman, A. (deposition date: 2017-06-12, release date: 2017-10-18, Last modification date: 2024-01-17)
Primary citationRadu, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.4 Å)
Structure validation

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