5Z41

Aquifex aeolicus MutL endonuclease domain with a single zinc ion.

Summary for 5Z41

• Entry DOI: 10.2210/pdb5z41/pdb
• Descriptor: DNA mismatch repair protein MutL, ZINC ION, MAGNESIUM ION, ... (5 entities in total)
• Functional Keywords: mismatch repair protein, endonuclease, zinc, thermophile, dna binding protein
• Biological source: Aquifex aeolicus VF5
• Total number of polymer chains: 1
• Total formula weight: 12678.52

Authors

Fukui, K.,Yano, T. (deposition date: 2018-01-10, release date: 2018-04-25, Last modification date: 2024-03-27)

Primary citation

Fukui, K.,Baba, S.,Kumasaka, T.,Yano, T.
Multiple zinc ions maintain the open conformation of the catalytic site in the DNA mismatch repair endonuclease MutL from Aquifex aeolicus
FEBS Lett., 592:1611-1619, 2018

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.

PubMed: 29645090
DOI: 10.1002/1873-3468.13050

Experimental method

X-RAY DIFFRACTION (1.7 Å)