1P49
Structure of Human Placental Estrone/DHEA Sulfatase
1P49 の概要
| エントリーDOI | 10.2210/pdb1p49/pdb |
| 分子名称 | STERYL-SULFATASE, octyl beta-D-glucopyranoside, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (6 entities in total) |
| 機能のキーワード | steroid biosynthesis, steroid sulfatase, estrone sulfate, dehydroepiandrosterone sulfate, human placental enzyme, endoplasmic reticulum membrane-bound, hydrolase |
| 由来する生物種 | Homo sapiens (human) |
| 細胞内の位置 | Endoplasmic reticulum membrane; Multi-pass membrane protein: P08842 |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 64214.03 |
| 構造登録者 | Hernandez-Guzman, F.G.,Higashiyama, T.,Pangborn, W.,Osawa, Y.,Ghosh, D. (登録日: 2003-04-21, 公開日: 2003-08-12, 最終更新日: 2025-03-26) |
| 主引用文献 | Hernandez-Guzman, F.G.,Higashiyama, T.,Pangborn, W.,Osawa, Y.,Ghosh, D. Structure of Human Estrone Sulfatase Suggests Functional Roles of Membrane Association J.Biol.Chem., 278:22989-22997, 2003 Cited by PubMed Abstract: Estrone sulfatase (ES; 562 amino acids), one of the key enzymes responsible for maintaining high levels of estrogens in breast tumor cells, is associated with the membrane of the endoplasmic reticulum (ER). The structure of ES, purified from the microsomal fraction of human placentas, has been determined at 2.60-A resolution by x-ray crystallography. This structure shows a domain consisting of two antiparallel alpha-helices that protrude from the roughly spherical molecule, thereby giving the molecule a "mushroom-like" shape. These highly hydrophobic helices, each about 40 A long, are capable of traversing the membrane, thus presumably anchoring the functional domain on the membrane surface facing the ER lumen. The location of the transmembrane domain is such that the opening to the active site, buried deep in a cavity of the "gill" of the "mushroom," rests near the membrane surface, thereby suggesting a role of the lipid bilayer in catalysis. This simple architecture could be a prototype utilized by the ER membrane in dictating the form and the function of ER-resident enzymes. PubMed: 12657638DOI: 10.1074/jbc.M211497200 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.6 Å) |
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