2OWY

The recombination-associated protein RdgC adopts a novel toroidal architecture for DNA binding

2OWY の概要

• エントリーDOI: 10.2210/pdb2owy/pdb
• 分子名称: Recombination-associated protein rdgC (1 entity in total)
• 機能のキーワード: homologous recombination, pseudomonas aeruginosa, rdgc, reca, ring-shaped dna binding proteins, dna binding protein
• 由来する生物種: Pseudomonas aeruginosa
• 細胞内の位置: Cytoplasm, nucleoid : Q9HYX7
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 68113.73

構造登録者

Suh, S.W. (登録日: 2007-02-17, 公開日: 2007-11-20, 最終更新日: 2024-03-13)

主引用文献

Ha, J.Y.,Kim, H.K.,Kim, D.J.,Kim, K.H.,Oh, S.J.,Lee, H.H.,Yoon, H.J.,Song, H.K.,Suh, S.W.
The recombination-associated protein RdgC adopts a novel toroidal architecture for DNA binding
Nucleic Acids Res., 35:2671-2681, 2007

PubMed Abstract: RecA plays a central role in the nonmutagenic repair of stalled replication forks in bacteria. RdgC, a recombination-associated DNA-binding protein, is a potential negative regulator of RecA function. Here, we have determined the crystal structure of RdgC from Pseudomonas aeruginosa. The J-shaped monomer has a unique fold and can be divided into three structural domains: tip domain, center domain and base domain. Two such monomers dimerize to form a ring-shaped molecule of approximate 2-fold symmetry. Of the two inter-subunit interfaces within the dimer, one interface ('interface A') between tip/center domains is more nonpolar than the other ('interface B') between base domains. The structure allows us to propose that the RdgC dimer binds dsDNA through the central hole of approximately 30 A diameter. The proposed model is supported by our DNA-binding assays coupled with mutagenesis, which indicate that the conserved positively charged residues on the protein surface around the central hole play important roles in DNA binding. The novel ring-shaped architecture of the RdgC dimer has significant implications for its role in homologous recombination.

PubMed: 17426134
DOI: 10.1093/nar/gkm144

実験手法

X-RAY DIFFRACTION (2.5 Å)