5Z42

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

(2018) FEBS Lett 592: 1611-1619

• PubMed: 29645090 Search on PubMed
• DOI: https://doi.org/10.1002/1873-3468.13050
• Primary Citation of Related Structures:  
  5Z41, 5Z42


• 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.

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Organizational Affiliation: 

Department of Biochemistry, Osaka Medical College, Takatsuki, Japan.