4ZYG
Crystal structure of methylated Sulfolobus solfataricus O6-methylguanine methyltransferase
Summary for 4ZYG
| Entry DOI | 10.2210/pdb4zyg/pdb |
| Descriptor | Methylated-DNA--protein-cysteine methyltransferase (2 entities in total) |
| Functional Keywords | extremophiles, dna repair, alkylated dna-protein alkyltransferase, methylated protein, transferase |
| Biological source | Sulfolobus solfataricus |
| Cellular location | Cytoplasm : Q97VW7 |
| Total number of polymer chains | 2 |
| Total formula weight | 34148.18 |
| Authors | Miggiano, R.,Rossi, F.,Rizzi, M. (deposition date: 2015-05-21, release date: 2015-08-12, Last modification date: 2024-01-10) |
| Primary citation | Perugino, G.,Miggiano, R.,Serpe, M.,Vettone, A.,Valenti, A.,Lahiri, S.,Rossi, F.,Rossi, M.,Rizzi, M.,Ciaramella, M. Structure-function relationships governing activity and stability of a DNA alkylation damage repair thermostable protein. Nucleic Acids Res., 43:8801-8816, 2015 Cited by PubMed Abstract: Alkylated DNA-protein alkyltransferases repair alkylated DNA bases, which are among the most common DNA lesions, and are evolutionary conserved, from prokaryotes to higher eukaryotes. The human ortholog, hAGT, is involved in resistance to alkylating chemotherapy drugs. We report here on the alkylated DNA-protein alkyltransferase, SsOGT, from an archaeal species living at high temperature, a condition that enhances the harmful effect of DNA alkylation. The exceptionally high stability of SsOGT gave us the unique opportunity to perform structural and biochemical analysis of a protein of this class in its post-reaction form. This analysis, along with those performed on SsOGT in its ligand-free and DNA-bound forms, provides insights in the structure-function relationships of the protein before, during and after DNA repair, suggesting a molecular basis for DNA recognition, catalytic activity and protein post-reaction fate, and giving hints on the mechanism of alkylation-induced inactivation of this class of proteins. PubMed: 26227971DOI: 10.1093/nar/gkv774 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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