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Multiple zinc ions maintain the open conformation of the catalytic site in the DNA mismatch repair endonuclease MutL from Aquifex aeolicus
Author(s) -
Fukui Kenji,
Baba Seiki,
Kumasaka Takashi,
Yano Takato
Publication year - 2018
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1002/1873-3468.13050
Subject(s) - endonuclease , aquifex aeolicus , chemistry , dna , biophysics , biochemistry , biology , escherichia coli , gene
The DNA mismatch repair endonuclease MutL consists of N‐terminal ATP ase 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.