5ZYW
The crystal structure of apo-HsMGME1 with Mn2+
Summary for 5ZYW
| Entry DOI | 10.2210/pdb5zyw/pdb |
| Descriptor | Mitochondrial genome maintenance exonuclease 1, MANGANESE (II) ION, L(+)-TARTARIC ACID, ... (5 entities in total) |
| Functional Keywords | huamnmgme1, dna complex, dna exonuclease, dna binding protein, hydrolase |
| Biological source | Homo sapiens (Human) |
| Total number of polymer chains | 1 |
| Total formula weight | 29924.52 |
| Authors | |
| Primary citation | Yang, C.,Wu, R.,Liu, H.,Chen, Y.,Gao, Y.,Chen, X.,Li, Y.,Ma, J.,Li, J.,Gan, J. Structural insights into DNA degradation by human mitochondrial nuclease MGME1 Nucleic Acids Res., 46:11075-11088, 2018 Cited by PubMed Abstract: Mitochondrial nucleases play important roles in accurate maintenance and correct metabolism of mtDNA, the own genetic materials of mitochondria that are passed exclusively from mother to child. MGME1 is a highly conserved DNase that was discovered recently. Mutations in MGME1-coding gene lead to severe mitochondrial syndromes characterized by external ophthalmoplegia, emaciation, and respiratory failure in humans. Unlike many other nucleases that are distributed in multiple cellular organelles, human MGME1 is a mitochondria-specific nuclease; therefore, it can serve as an ideal target for treating related syndromes. Here, we report one HsMGME1-Mn2+ complex and three different HsMGME1-DNA complex structures. In combination with in vitro cleavage assays, our structures reveal the detailed molecular basis for substrate DNA binding and/or unwinding by HsMGME1. Besides the conserved two-cation-assisted catalytic mechanism, structural analysis of HsMGME1 and comparison with homologous proteins also clarified substrate binding and cleavage directionalities of the DNA double-strand break repair complexes RecBCD and AddAB. PubMed: 30247721DOI: 10.1093/nar/gky855 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.2 Å) |
Structure validation
Download full validation report
