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7M2U

Nucleotide Excision Repair complex TFIIH Rad4-33

7M2U の概要
エントリーDOI10.2210/pdb7m2u/pdb
EMDBエントリー22576
分子名称DNA repair helicase RAD25, DNA repair protein RAD33, General transcription and DNA repair factor IIH subunit TFB2, ... (14 entities in total)
機能のキーワードner, nucleotide excision repair, tfiih, rad4, xpc, nuclear protein, nuclear protein-dna complex, nuclear protein/dna
由来する生物種Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast)
詳細
タンパク質・核酸の鎖数11
化学式量合計529983.10
構造登録者
van Eeuwen, T.,Murakami, K. (登録日: 2021-03-17, 公開日: 2021-07-28, 最終更新日: 2025-05-14)
主引用文献van Eeuwen, T.,Shim, Y.,Kim, H.J.,Zhao, T.,Basu, S.,Garcia, B.A.,Kaplan, C.D.,Min, J.H.,Murakami, K.
Cryo-EM structure of TFIIH/Rad4-Rad23-Rad33 in damaged DNA opening in nucleotide excision repair.
Nat Commun, 12:3338-3338, 2021
Cited by
PubMed Abstract: The versatile nucleotide excision repair (NER) pathway initiates as the XPC-RAD23B-CETN2 complex first recognizes DNA lesions from the genomic DNA and recruits the general transcription factor complex, TFIIH, for subsequent lesion verification. Here, we present a cryo-EM structure of an NER initiation complex containing Rad4-Rad23-Rad33 (yeast homologue of XPC-RAD23B-CETN2) and 7-subunit coreTFIIH assembled on a carcinogen-DNA adduct lesion at 3.9-9.2 Å resolution. A ~30-bp DNA duplex could be mapped as it straddles between Rad4 and the Ssl2 (XPB) subunit of TFIIH on the 3' and 5' side of the lesion, respectively. The simultaneous binding with Rad4 and TFIIH was permitted by an unwinding of DNA at the lesion. Translocation coupled with torque generation by Ssl2 and Rad4 would extend the DNA unwinding at the lesion and deliver the damaged strand to Rad3 (XPD) in an open form suitable for subsequent lesion scanning and verification.
PubMed: 34099686
DOI: 10.1038/s41467-021-23684-x
主引用文献が同じPDBエントリー
実験手法
ELECTRON MICROSCOPY (8.2 Å)
構造検証レポート
Validation report summary of 7m2u
検証レポート(詳細版)ダウンロードをダウンロード

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件を2026-04-15に公開中

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