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 Lettjournal_title
FEBS lettersauthors
Fukui K,Baba S,Kumasaka T,Yano Tdoi
10.1002/1873-3468.13050subject
Has Abstractpub_date
2018-05-01 00:00:00pages
1611-1619issue
9eissn
0014-5793issn
1873-3468journal_volume
592pub_type
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