6M9M
Streptococcus mutans AlkD2 bound to inosine-5'-monophosphate
Summary for 6M9M
| Entry DOI | 10.2210/pdb6m9m/pdb |
| Descriptor | AlkD2, INOSINIC ACID, CHLORIDE ION, ... (4 entities in total) |
| Functional Keywords | heat-like repeat, nucleotide binding, unknown function |
| Biological source | Streptococcus mutans |
| Total number of polymer chains | 1 |
| Total formula weight | 24966.92 |
| Authors | Eichman, B.F.,Shi, R. (deposition date: 2018-08-23, release date: 2018-10-10, Last modification date: 2023-10-11) |
| Primary citation | Shi, R.,Shen, X.X.,Rokas, A.,Eichman, B.F. Structural Biology of the HEAT-Like Repeat Family of DNA Glycosylases. Bioessays, 40:e1800133-e1800133, 2018 Cited by PubMed Abstract: DNA glycosylases remove aberrant DNA nucleobases as the first enzymatic step of the base excision repair (BER) pathway. The alkyl-DNA glycosylases AlkC and AlkD adopt a unique structure based on α-helical HEAT repeats. Both enzymes identify and excise their substrates without a base-flipping mechanism used by other glycosylases and nucleic acid processing proteins to access nucleobases that are otherwise stacked inside the double-helix. Consequently, these glycosylases act on a variety of cationic nucleobase modifications, including bulky adducts, not previously associated with BER. The related non-enzymatic HEAT-like repeat (HLR) proteins, AlkD2, and AlkF, have unique nucleic acid binding properties that expand the functions of this relatively new protein superfamily beyond DNA repair. Here, we review the phylogeny, biochemistry, and structures of the HLR proteins, which have helped broaden our understanding of the mechanisms by which DNA glycosylases locate and excise chemically modified DNA nucleobases. PubMed: 30264543DOI: 10.1002/bies.201800133 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.401 Å) |
Structure validation
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