4CIS
Structure of MutM in complex with carbocyclic 8-oxo-G containing DNA
Summary for 4CIS
| Entry DOI | 10.2210/pdb4cis/pdb |
| Descriptor | FORMAMIDOPYRIMIDIN DNA GLYCOSYLASE, DNA, ZINC ION, ... (6 entities in total) |
| Functional Keywords | hydrolase, base excision repair, dna repair |
| Biological source | Lactococcus lactis subsp. cremoris More |
| Total number of polymer chains | 4 |
| Total formula weight | 73918.25 |
| Authors | Schneider, S.,Sadeghian, K.,Flaig, D.,Blank, I.D.,Strasser, R.,Stathis, D.,Winnacker, M.,Carell, T.,Ochsenfeld, C. (deposition date: 2013-12-15, release date: 2014-06-04, Last modification date: 2023-12-20) |
| Primary citation | Sadeghian, K.,Flaig, D.,Blank, I.D.,Schneider, S.,Strasser, R.,Stathis, D.,Winnacker, M.,Carell, T.,Ochsenfeld, C. Ribose-protonated DNA base excision repair: a combined theoretical and experimental study. Angew. Chem. Int. Ed. Engl., 53:10044-10048, 2014 Cited by PubMed Abstract: Living organisms protect the genome against external influences by recognizing and repairing damaged DNA. A common source of gene mutation is the oxidized guanine, which undergoes base excision repair through cleavage of the glycosidic bond between the ribose and the nucleobase of the lesion. We unravel the repair mechanism utilized by bacterial glycosylase, MutM, using quantum-chemical calculations involving more than 1000 atoms of the catalytic site. In contrast to the base-protonated pathway currently favored in the literature, we show that the initial protonation of the lesion's ribose paves the way for an almost barrier-free glycosidic cleavage. The combination of theoretical and experimental data provides further insight into the selectivity and discrimination of MutM's binding site toward various substrates. PubMed: 25065673DOI: 10.1002/anie.201403334 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.05 Å) |
Structure validation
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