2PMT
GLUTATHIONE TRANSFERASE FROM PROTEUS MIRABILIS
2PMT の概要
エントリーDOI | 10.2210/pdb2pmt/pdb |
分子名称 | GLUTATHIONE TRANSFERASE, GLUTATHIONE (2 entities in total) |
機能のキーワード | transferase, glutathione-conjugating, a putative oxidoreductase |
由来する生物種 | Proteus mirabilis |
細胞内の位置 | Cytoplasm: P15214 |
タンパク質・核酸の鎖数 | 4 |
化学式量合計 | 92754.27 |
構造登録者 | Rossjohn, J.,Polekhina, G.,Feil, S.C.,Allocati, N.,Masulli, M.,Diilio, C.,Parker, M.W. (登録日: 1998-04-28, 公開日: 1999-04-27, 最終更新日: 2024-06-05) |
主引用文献 | Rossjohn, J.,Polekhina, G.,Feil, S.C.,Allocati, N.,Masulli, M.,De Illio, C.,Parker, M.W. A mixed disulfide bond in bacterial glutathione transferase: functional and evolutionary implications. Structure, 6:721-734, 1998 Cited by PubMed Abstract: Glutathione S-transferases (GSTs) are a multifunctional group of enzymes, widely distributed in aerobic organisms, that have a critical role in the cellular detoxification process. Unlike their mammalian counterparts, bacterial GSTs often catalyze quite specific reactions, suggesting that their roles in bacteria might be different. The GST from Proteus mirabilis (PmGST B1-1) is known to bind certain antibiotics tightly and reduce the antimicrobial activity of beta-lactam drugs. Hence, bacterial GSTs may play a part in bacterial resistance towards antibiotics and are the subject of intense interest. PubMed: 9655824DOI: 10.1016/S0969-2126(98)00074-4 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2.7 Å) |
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