6RO4

Structure of the core TFIIH-XPA-DNA complex

6RO4 の概要

• エントリーDOI: 10.2210/pdb6ro4/pdb
• EMDBエントリー: 4970
• 分子名称: DNA1, IRON/SULFUR CLUSTER, ZINC ION, ... (11 entities in total)
• 機能のキーワード: complex, helicase, translocase, dna repair
• 由来する生物種: Homo sapiens (Human); 詳細
• タンパク質・核酸の鎖数: 9
• 化学式量合計: 377907.84

構造登録者

Kokic, G.,Chernev, A.,Tegunov, D.,Dienemann, C.,Urlaub, H.,Cramer, P. (登録日: 2019-05-10, 公開日: 2019-07-03, 最終更新日: 2024-05-22)

主引用文献

Kokic, G.,Chernev, A.,Tegunov, D.,Dienemann, C.,Urlaub, H.,Cramer, P.
Structural basis of TFIIH activation for nucleotide excision repair.
Nat Commun, 10:2885-2885, 2019

PubMed Abstract: Nucleotide excision repair (NER) is the major DNA repair pathway that removes UV-induced and bulky DNA lesions. There is currently no structure of NER intermediates, which form around the large multisubunit transcription factor IIH (TFIIH). Here we report the cryo-EM structure of an NER intermediate containing TFIIH and the NER factor XPA. Compared to its transcription conformation, the TFIIH structure is rearranged such that its ATPase subunits XPB and XPD bind double- and single-stranded DNA, consistent with their translocase and helicase activities, respectively. XPA releases the inhibitory kinase module of TFIIH, displaces a 'plug' element from the DNA-binding pore in XPD, and together with the NER factor XPG stimulates XPD activity. Our results explain how TFIIH is switched from a transcription to a repair factor, and provide the basis for a mechanistic analysis of the NER pathway.

PubMed: 31253769
DOI: 10.1038/s41467-019-10745-5

実験手法

ELECTRON MICROSCOPY (3.5 Å)