6NMI

Cryo-EM structure of the human TFIIH core complex

Summary for 6NMI

• Entry DOI: 10.2210/pdb6nmi/pdb
• EMDB information: 0452
• Descriptor: General transcription and DNA repair factor IIH helicase subunit XPB, ZINC ION, General transcription and DNA repair factor IIH helicase subunit XPD, ... (10 entities in total)
• Functional Keywords: transcription, dna repair, helicase, multiprotein complex
• Biological source: Homo sapiens (Human); More
• Total number of polymer chains: 8
• Total formula weight: 389388.94

Authors

Greber, B.J.,Toso, D.,Fang, J.,Nogales, E. (deposition date: 2019-01-10, release date: 2019-03-13, Last modification date: 2024-11-06)

Primary citation

Greber, B.J.,Toso, D.B.,Fang, J.,Nogales, E.
The complete structure of the human TFIIH core complex.
Elife, 8:-, 2019

PubMed Abstract: Transcription factor IIH (TFIIH) is a heterodecameric protein complex critical for transcription initiation by RNA polymerase II and nucleotide excision DNA repair. The TFIIH core complex is sufficient for its repair functions and harbors the XPB and XPD DNA-dependent ATPase/helicase subunits, which are affected by human disease mutations. Transcription initiation additionally requires the CdK activating kinase subcomplex. Previous structural work has provided only partial insight into the architecture of TFIIH and its interactions within transcription pre-initiation complexes. Here, we present the complete structure of the human TFIIH core complex, determined by phase-plate cryo-electron microscopy at 3.7 Å resolution. The structure uncovers the molecular basis of TFIIH assembly, revealing how the recruitment of XPB by p52 depends on a pseudo-symmetric dimer of homologous domains in these two proteins. The structure also suggests a function for p62 in the regulation of XPD, and allows the mapping of previously unresolved human disease mutations.

PubMed: 30860024
DOI: 10.7554/eLife.44771

Experimental method

ELECTRON MICROSCOPY (3.7 Å)