3K75

X-ray crystal structure of reduced XRCC1 bound to DNA pol beta catalytic domain

3K75 の概要

• エントリーDOI: 10.2210/pdb3k75/pdb
• 関連するPDBエントリー: 3K76 3K77
• 分子名称: DNA repair protein XRCC1, DNA polymerase beta (2 entities in total)
• 機能のキーワード: allosteric disulfide, xrcc1, pol beta, dna damage, dna repair, nucleus, phosphoprotein, dna replication, dna synthesis, dna-binding, dna-directed dna polymerase, lyase, magnesium, metal-binding, methylation, nucleotidyltransferase, transferase, dna-binding protein, dna binding protein
• 由来する生物種: Homo sapiens (human); 詳細
• 細胞内の位置: Nucleus: P18887 P06766
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 100793.28

構造登録者

Cuneo, M.J.,London, R.E. (登録日: 2009-10-12, 公開日: 2010-04-28, 最終更新日: 2024-02-21)

主引用文献

Cuneo, M.J.,London, R.E.
Oxidation state of the XRCC1 N-terminal domain regulates DNA polymerase beta binding affinity.
Proc.Natl.Acad.Sci.USA, 107:6805-6810, 2010

PubMed Abstract: Formation of a complex between the XRCC1 N-terminal domain (NTD) and DNA polymerase beta (Pol beta) is central to base excision repair of damaged DNA. Two crystal forms of XRCC1-NTD complexed with Pol beta have been solved, revealing that the XRCC1-NTD is able to adopt a redox-dependent alternate fold, characterized by a disulfide bond, and substantial variations of secondary structure, folding topology, and electrostatic surface. Although most of these structural changes occur distal to the interface, the oxidized XRCC1-NTD forms additional interactions with Pol beta, enhancing affinity by an order of magnitude. Transient disulfide bond formation is increasingly recognized as an important molecular regulatory mechanism. The results presented here suggest a paradigm in DNA repair in which the redox state of a scaffolding protein plays an active role in organizing the repair complex.

PubMed: 20351257
DOI: 10.1073/pnas.0914077107

実験手法

X-RAY DIFFRACTION (2.95 Å)