5OF4

The cryo-EM structure of human TFIIH

5OF4 の概要

• エントリーDOI: 10.2210/pdb5of4/pdb
• EMDBエントリー: 3802
• 分子名称: TFIIH basal transcription factor complex helicase XPB subunit,XPB,TFIIH basal transcription factor complex helicase XPB subunit, Unassigned secondary structure elements (XPB NTE region), IRON/SULFUR CLUSTER, ... (11 entities in total)
• 機能のキーワード: transcription initiation, dna repair, multiprotein complex, kinase, helicase, transcription
• 由来する生物種: Homo sapiens (Human); 詳細
• タンパク質・核酸の鎖数: 10
• 化学式量合計: 306618.26

構造登録者

Greber, B.J.,Nguyen, T.H.D.,Fang, J.,Afonine, P.V.,Adams, P.D.,Nogales, E. (登録日: 2017-07-10, 公開日: 2017-09-13, 最終更新日: 2024-11-13)

主引用文献

Greber, B.J.,Nguyen, T.H.D.,Fang, J.,Afonine, P.V.,Adams, P.D.,Nogales, E.
The cryo-electron microscopy structure of human transcription factor IIH.
Nature, 549:414-417, 2017

PubMed Abstract: Human transcription factor IIH (TFIIH) is part of the general transcriptional machinery required by RNA polymerase II for the initiation of eukaryotic gene transcription. Composed of ten subunits that add up to a molecular mass of about 500 kDa, TFIIH is also essential for nucleotide excision repair. The seven-subunit TFIIH core complex formed by XPB, XPD, p62, p52, p44, p34, and p8 is competent for DNA repair, while the CDK-activating kinase subcomplex, which includes the kinase activity of CDK7 as well as the cyclin H and MAT1 subunits, is additionally required for transcription initiation. Mutations in the TFIIH subunits XPB, XPD, and p8 lead to severe premature ageing and cancer propensity in the genetic diseases xeroderma pigmentosum, Cockayne syndrome, and trichothiodystrophy, highlighting the importance of TFIIH for cellular physiology. Here we present the cryo-electron microscopy structure of human TFIIH at 4.4 Å resolution. The structure reveals the molecular architecture of the TFIIH core complex, the detailed structures of its constituent XPB and XPD ATPases, and how the core and kinase subcomplexes of TFIIH are connected. Additionally, our structure provides insight into the conformational dynamics of TFIIH and the regulation of its activity.

PubMed: 28902838
DOI: 10.1038/nature23903

実験手法

ELECTRON MICROSCOPY (4.4 Å)