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FEBS Lett. 2018 May;592(9):1611-1619. doi: 10.1002/1873-3468.13050. Epub 2018 Apr 22.

Multiple zinc ions maintain the open conformation of the catalytic site in the DNA mismatch repair endonuclease MutL from Aquifex aeolicus.

Author information

1
Department of Biochemistry, Osaka Medical College, Takatsuki, Japan.
2
Japan Synchrotron Radiation Research Institute (JASRI), SPring-8, Sayo, Japan.

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.

KEYWORDS:

DNA mismatch repair; endonuclease; zinc

PMID:
29645090
DOI:
10.1002/1873-3468.13050
[Indexed for MEDLINE]

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