5Z42

Aquifex aeolicus MutL endonuclease domain with three zinc ions.

5Z42 の概要

• エントリーDOI: 10.2210/pdb5z42/pdb
• 分子名称: DNA mismatch repair protein MutL, ZINC ION, SODIUM ION, ... (7 entities in total)
• 機能のキーワード: mismatch repair protein, endonuclease, zinc, thermophile, dna binding protein
• 由来する生物種: Aquifex aeolicus (strain VF5)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 12891.16

構造登録者

Fukui, K.,Yano, T. (登録日: 2018-01-10, 公開日: 2018-04-25, 最終更新日: 2024-03-27)

主引用文献

Fukui, K.,Baba, S.,Kumasaka, T.,Yano, T.
Multiple zinc ions maintain the open conformation of the catalytic site in the DNA mismatch repair endonuclease MutL from Aquifex aeolicus
FEBS Lett., 592:1611-1619, 2018

PubMed Abstract: The DNA mismatch repair endonuclease MutL consists of N-terminal ATPase and C-terminal endonuclease domains. The endonuclease domain binds zinc ion, although the ion seems not to function as a catalytic metal ion. Here, we solved the crystal structures of the Aquifex aeolicus MutL (aqMutL) endonuclease domain complexed with a single and three zinc ions. Differences between the two structures show that binding of multiple zinc ions induces a closed-to-open conformational change at the catalytic site. It is also revealed that the three-zinc-bound form of the endonuclease domain exhibits higher endonuclease activity than the single-zinc-bound form. These results indicate that multiple zinc ions are required for the proper folding of the endonuclease domain, which would facilitate the endonuclease activity of aqMutL.

PubMed: 29645090
DOI: 10.1002/1873-3468.13050

実験手法

X-RAY DIFFRACTION (1.3 Å)