5G32

Structure of Rad14 in complex with acetylaminophenyl-guanine containing DNA

5G32 の概要

• エントリーDOI: 10.2210/pdb5g32/pdb
• 関連するPDBエントリー: 5G33 5G34 5G35
• 分子名称: RAD14, 5'-D(*GP*CP*TP*CP*TP*AP*6FKP*TP*CP*AP*TP*CP*AP*CP)-3', 5'-D(*GP*TP*GP*AP*TP*GP*AP*CP*GP*TP*AP*GP*AP*GP)-3', ... (5 entities in total)
• 機能のキーワード: cell cycle, dna repair, nucleotide excision repair
• 由来する生物種: SACCHAROMYCES CEREVISIAE (BAKER'S YEAST); 詳細
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 49402.17

構造登録者

Simon, N.,Ebert, C.,Schneider, S. (登録日: 2016-04-18, 公開日: 2016-06-01, 最終更新日: 2024-05-08)

主引用文献

Schneider, S.,Simon, N.,Ebert, C.
Structural Basis for Bulky Adduct DNA Lesion Recognition by the Nucleotide Excision Repair Protein Rad14.
Chemistry, 22:10782-, 2016

PubMed Abstract: Heterocyclic aromatic amines react with purine bases and result in bulky DNA adducts that cause mutations. Such structurally diverse lesions are substrates for the nucleotide excision repair (NER). It is thought that the NER machinery recognises and verifies distorted DNA conformations, also involving the xeroderma pigmentosum group A and C proteins (XPA, XPC) that act as a scaffold between the DNA substrate and several other NER proteins. Here we present the synthesis of DNA molecules containing the polycyclic, aromatic amine C8-guanine lesions acetylaminophenyl, acetylaminonaphthyl, acetylaminoanthryl, and acetylaminopyrenyl, as well as their crystal structures in complex with the yeast XPA homologue Rad14. This work further substantiates the indirect lesion-detection mechanism employed by the NER system that recognises destabilised and deformable DNA structures.

PubMed: 27223336
DOI: 10.1002/CHEM.201602438

実験手法

X-RAY DIFFRACTION (2.2 Å)