6TC9
Crystal structure of MutM from Neisseria meningitidis
Summary for 6TC9
| Entry DOI | 10.2210/pdb6tc9/pdb |
| Related | 6TC6 |
| Descriptor | DNA containing abasic site analogue, Formamidopyrimidine-DNA glycosylase, DNA, ... (6 entities in total) |
| Functional Keywords | mutm, fpg/nei, neisseria meningitidis, ber, dna repair, dna binding protein |
| Biological source | Neisseria meningitidis alpha522 More |
| Total number of polymer chains | 6 |
| Total formula weight | 78785.52 |
| Authors | Silhan, J.,Landova, B.,Boura, E. (deposition date: 2019-11-05, release date: 2020-09-16, Last modification date: 2024-01-24) |
| Primary citation | Landova, B.,Silhan, J. Conformational changes of DNA repair glycosylase MutM triggered by DNA binding. Febs Lett., 594:3032-3044, 2020 Cited by PubMed Abstract: Bacterial MutM is a DNA repair glycosylase removing DNA damage generated from oxidative stress and, therefore, preventing mutations and genomic instability. MutM belongs to the Fpg/Nei family of prokaryotic enzymes sharing structural and functional similarities with their eukaryotic counterparts, for example, NEIL1-NEIL3. Here, we present two crystal structures of MutM from pathogenic Neisseria meningitidis: a MutM holoenzyme and MutM bound to DNA. The free enzyme exists in an open conformation, while upon binding to DNA, both the enzyme and DNA undergo substantial structural changes and domain rearrangement. Our data show that not only NEI glycosylases but also the MutMs undergo dramatic conformational changes. Moreover, crystallographic data support the previously published observations that MutM enzymes are rather flexible and dynamic molecules. PubMed: 32598485DOI: 10.1002/1873-3468.13876 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.175 Å) |
Structure validation
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