5LLQ
Crystal structure of Sulfolobus solfataricus O6-methylguanine methyltransferase C119F variant
Summary for 5LLQ
| Entry DOI | 10.2210/pdb5llq/pdb |
| Descriptor | Methylated-DNA--protein-cysteine methyltransferase, GLYCEROL (3 entities in total) |
| Functional Keywords | dna dealkylation, ogt, inactive mutant, transferase |
| Biological source | Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2) |
| Cellular location | Cytoplasm : Q97VW7 |
| Total number of polymer chains | 2 |
| Total formula weight | 37541.80 |
| Authors | Miggiano, R.,Rossi, F.,Rizzi, M. (deposition date: 2016-07-28, release date: 2016-11-09, Last modification date: 2024-01-10) |
| Primary citation | Morrone, C.,Miggiano, R.,Serpe, M.,Massarotti, A.,Valenti, A.,Del Monaco, G.,Rossi, M.,Rossi, F.,Rizzi, M.,Perugino, G.,Ciaramella, M. Interdomain interactions rearrangements control the reaction steps of a thermostable DNA alkyltransferase. Biochim.Biophys.Acta, 1861:86-96, 2016 Cited by PubMed Abstract: Alkylated DNA-protein alkyltransferases (AGTs) are conserved proteins that repair alkylation damage in DNA by using a single-step mechanism leading to irreversible alkylation of the catalytic cysteine in the active site. Trans-alkylation induces inactivation and destabilization of the protein, both in vitro and in vivo, likely triggering conformational changes. A complete picture of structural rearrangements occurring during the reaction cycle is missing, despite considerable interest raised by the peculiarity of AGT reaction, and the contribution of a functional AGT in limiting the efficacy of chemotherapy with alkylating drugs. PubMed: 27777086DOI: 10.1016/j.bbagen.2016.10.020 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.7 Å) |
Structure validation
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