3TAL

Crystal structure of NurA with manganese

3TAL の概要

• エントリーDOI: 10.2210/pdb3tal/pdb
• 関連するPDBエントリー: 3TAI 3TAZ
• 分子名称: DNA double-strand break repair protein nurA, MANGANESE (II) ION, GLYCEROL, ... (4 entities in total)
• 機能のキーワード: recombination, hydrolase
• 由来する生物種: Pyrococcus furiosus
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 108868.02

構造登録者

Chae, J.,Kim, Y.C.,Cho, Y. (登録日: 2011-08-04, 公開日: 2011-11-23, 最終更新日: 2024-10-30)

主引用文献

Chae, J.,Kim, Y.C.,Cho, Y.
Crystal structure of the NurA-dAMP-Mn2+ complex
Nucleic Acids Res., 40:2258-2270, 2012

PubMed Abstract: Generation of the 3' overhang is a critical event during homologous recombination (HR) repair of DNA double strand breaks. A 5'-3' nuclease, NurA, plays an important role in generating 3' single-stranded DNA during archaeal HR, together with Mre11-Rad50 and HerA. We have determined the crystal structures of apo- and dAMP-Mn(2)(+)-bound NurA from Pyrococcus furiousus (Pf NurA) to provide the basis for its cleavage mechanism. Pf NurA forms a pyramid-shaped dimer containing a large central channel on one side, which becomes narrower towards the peak of the pyramid. The structure contains a PIWI domain with high similarity to argonaute, endoV nuclease and RNase H. The two active sites, each of which contains Mn(2)(+) ion(s) and dAMP, are at the corners of the elliptical channel near the flat face of the dimer. The 3' OH group of the ribose ring is directed toward the channel entrance, explaining the 5'-3' nuclease activity of Pf NurA. We provide a DNA binding and cleavage model for Pf NurA.

PubMed: 22064858
DOI: 10.1093/nar/gkr999

実験手法

X-RAY DIFFRACTION (3.15 Å)