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4ZYE

Crystal structure of Sulfolobus solfataricus O6-methylguanine methyltransferase

Summary for 4ZYE
Entry DOI10.2210/pdb4zye/pdb
DescriptorMethylated-DNA--protein-cysteine methyltransferase, GLYCEROL, NITRATE ION, ... (4 entities in total)
Functional Keywordstransferase, extremophiles, dna repair, alkylated dna-protein alkyltransferase
Biological sourceSulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
Cellular locationCytoplasm : Q97VW7
Total number of polymer chains1
Total formula weight19004.98
Authors
Miggiano, R.,Rossi, F.,Rizzi, M. (deposition date: 2015-05-21, release date: 2015-08-12, Last modification date: 2024-10-23)
Primary citationPerugino, 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: 26227971
DOI: 10.1093/nar/gkv774
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.85 Å)
Structure validation

226707

건을2024-10-30부터공개중

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