6M3T

Crystal structure of the mouse endonuclease EndoG(H138A/C110A), space group P41212

Summary for 6M3T

• Entry DOI: 10.2210/pdb6m3t/pdb
• Related: 6M3F
• Descriptor: Endonuclease G, mitochondrial, MAGNESIUM ION (3 entities in total)
• Functional Keywords: endog, dnase, apoptosis
• Biological source: Mus musculus (Mouse)
• Total number of polymer chains: 2
• Total formula weight: 54994.37

Authors

Park, K.H.,Woo, E.J. (deposition date: 2020-03-04, release date: 2020-08-12, Last modification date: 2023-11-29)

Primary citation

Park, K.H.,Yoon, S.M.,Song, H.N.,Yang, J.H.,Ryu, S.E.,Woo, E.J.
Crystal structure of the mouse endonuclease G.
Biochem.Biophys.Res.Commun., 526:35-40, 2020

PubMed Abstract: Endonuclease G (EndoG) is a mitochondrial enzyme that responds to apoptotic stimuli by translocating to the nucleus and cleaving the chromatin DNA. The molecular mechanism of EndoG still remains unknown in higher organisms. Here, we determined the crystal structure of mouse EndoG at ∼1.96 Å resolution. The EndoG shows an altered dimeric configuration in which N-terminal region of one subunit interact to the other subunit in dimer. The deletion of this region that is highly conserved in mammalian EndoGs resulted in a monomer with significantly reduced activity suggesting the association of the dimeric arrangement into the nuclease activity. Furthermore, we observed a large conformational change in the loop of the active site groove in EndoG, which corresponds to the DNA binding region. Intriguingly, EndoG dimers are linked by oxidation of the reactive cysteine 110 in this flexible loop to form a long oligomeric chain in the crystal lattice. The structural analysis and ensuing biochemical data suggest that this flexible loop region in the active site is important to the regulation of EndoG nuclease function in mouse.

PubMed: 32192768
DOI: 10.1016/j.bbrc.2020.03.060

Experimental method

X-RAY DIFFRACTION (2.38 Å)