2QSF

Crystal structure of the Rad4-Rad23 complex

2QSF の概要

• エントリーDOI: 10.2210/pdb2qsf/pdb
• 関連するPDBエントリー: 2QSG 2QSH
• 分子名称: DNA repair protein RAD4, UV excision repair protein RAD23 (3 entities in total)
• 機能のキーワード: alpha-beta structure, beta hairpin, transglutaminase fold, dna-damage recognition, dna repair, dna binding protein, nucleotide excision repair, xeroderma pigmentosum
• 由来する生物種: Saccharomyces cerevisiae (baker's yeast); 詳細
• 細胞内の位置: Cytoplasm: P14736; Nucleus: P32628
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 79923.45

構造登録者

Min, J.-H.,Pavletich, N.P. (登録日: 2007-07-31, 公開日: 2007-10-02, 最終更新日: 2024-02-21)

主引用文献

Min, J.-H.,Pavletich, N.P.
Recognition of DNA damage by the Rad4 nucleotide excision repair protein
Nature, 449:570-575, 2007

PubMed Abstract: Mutations in the nucleotide excision repair (NER) pathway can cause the xeroderma pigmentosum skin cancer predisposition syndrome. NER lesions are limited to one DNA strand, but otherwise they are chemically and structurally diverse, being caused by a wide variety of genotoxic chemicals and ultraviolet radiation. The xeroderma pigmentosum C (XPC) protein has a central role in initiating global-genome NER by recognizing the lesion and recruiting downstream factors. Here we present the crystal structure of the yeast XPC orthologue Rad4 bound to DNA containing a cyclobutane pyrimidine dimer (CPD) lesion. The structure shows that Rad4 inserts a beta-hairpin through the DNA duplex, causing the two damaged base pairs to flip out of the double helix. The expelled nucleotides of the undamaged strand are recognized by Rad4, whereas the two CPD-linked nucleotides become disordered. These findings indicate that the lesions recognized by Rad4/XPC thermodynamically destabilize the Watson-Crick double helix in a manner that facilitates the flipping-out of two base pairs.

PubMed: 17882165
DOI: 10.1038/nature06155

実験手法

X-RAY DIFFRACTION (2.35 Å)