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

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.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Fukui K,Baba S,Kumasaka T,Yano T

doi

10.1002/1873-3468.13050

subject

Has Abstract

pub_date

2018-05-01 00:00:00

pages

1611-1619

issue

9

eissn

0014-5793

issn

1873-3468

journal_volume

592

pub_type

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