4ZYE

Crystal structure of Sulfolobus solfataricus O6-methylguanine methyltransferase

4ZYE の概要

• エントリーDOI: 10.2210/pdb4zye/pdb
• 分子名称: Methylated-DNA--protein-cysteine methyltransferase, GLYCEROL, NITRATE ION, ... (4 entities in total)
• 機能のキーワード: transferase, extremophiles, dna repair, alkylated dna-protein alkyltransferase
• 由来する生物種: Sulfolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
• 細胞内の位置: Cytoplasm : Q97VW7
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 19004.98

構造登録者

Miggiano, R.,Rossi, F.,Rizzi, M. (登録日: 2015-05-21, 公開日: 2015-08-12, 最終更新日: 2024-10-23)

主引用文献

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

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

実験手法

X-RAY DIFFRACTION (1.85 Å)