2H8A
Structure of Microsomal Glutathione Transferase 1 in Complex with Glutathione
2H8A の概要
| エントリーDOI | 10.2210/pdb2h8a/pdb |
| 分子名称 | Microsomal glutathione S-transferase 1, GLUTATHIONE (2 entities in total) |
| 機能のキーワード | membrane protein, transferase |
| 由来する生物種 | Rattus norvegicus (Norway rat) |
| 細胞内の位置 | Microsome: P08011 |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 17668.61 |
| 構造登録者 | |
| 主引用文献 | Holm, P.J.,Bhakat, P.,Jegerschold, C.,Gyobu, N.,Mitsuoka, K.,Fujiyoshi, Y.,Morgenstern, R.,Hebert, H. Structural basis for detoxification and oxidative stress protection in membranes. J.Mol.Biol., 360:934-945, 2006 Cited by PubMed Abstract: Synthesis of mediators of fever, pain and inflammation as well as protection against reactive molecules and oxidative stress is a hallmark of the MAPEG superfamily (membrane associated proteins in eicosanoid and glutathione metabolism). The structure of a MAPEG member, rat microsomal glutathione transferase 1, at 3.2 A resolution, solved here in complex with glutathione by electron crystallography, defines the active site location and a cytosolic domain involved in enzyme activation. The glutathione binding site is found to be different from that of the canonical soluble glutathione transferases. The architecture of the homotrimer supports a catalytic mechanism involving subunit interactions and reveals both cytosolic and membraneous substrate entry sites, providing a rationale for the membrane location of the enzyme. PubMed: 16806268DOI: 10.1016/j.jmb.2006.05.056 主引用文献が同じPDBエントリー |
| 実験手法 | ELECTRON CRYSTALLOGRAPHY (3.2 Å) |
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