4DC9

Hexameric ring of Methanococcus voltae RadA

4DC9 の概要

• エントリーDOI: 10.2210/pdb4dc9/pdb
• 関連するPDBエントリー: 1T4G
• 分子名称: DNA repair and recombination protein radA, NITRATE ION (3 entities in total)
• 機能のキーワード: hexamer, rada, recombinase, homologous recombination, reca, dna binding protein
• 由来する生物種: Methanococcus voltae
• タンパク質・核酸の鎖数: 6
• 化学式量合計: 177109.70

構造登録者

Du, L.,Luo, Y. (登録日: 2012-01-17, 公開日: 2012-05-02, 最終更新日: 2023-09-13)

主引用文献

Du, L.,Luo, Y.
Structure of a hexameric form of RadA recombinase from Methanococcus voltae.
Acta Crystallogr.,Sect.F, 68:511-516, 2012

PubMed Abstract: Archaeal RadA proteins are close homologues of eukaryal Rad51 and DMC1 proteins and are remote homologues of bacterial RecA proteins. For the repair of double-stranded breaks in DNA, these recombinases promote a pivotal strand-exchange reaction between homologous single-stranded and double-stranded DNA substrates. This DNA-repair function also plays a key role in the resistance of cancer cells to chemotherapy and radiotherapy and in the resistance of bacterial cells to antibiotics. A hexameric form of a truncated Methanococcus voltae RadA protein devoid of its small N-terminal domain has been crystallized. The RadA hexamers further assemble into two-ringed assemblies. Similar assemblies can be observed in the crystals of Pyrococcus furiosus RadA and Homo sapiens DMC1. In all of these two-ringed assemblies the DNA-interacting L1 region of each protomer points inward towards the centre, creating a highly positively charged locus. The electrostatic characteristics of the central channels can be utilized in the design of novel recombinase inhibitors.

PubMed: 22691778
DOI: 10.1107/S1744309112010226

実験手法

X-RAY DIFFRACTION (2.6 Å)