1IGS
INDOLE-3-GLYCEROLPHOSPHATE SYNTHASE FROM SULFOLOBUS SOLFATARICUS AT 2.0 A RESOLUTION
1IGS の概要
エントリーDOI | 10.2210/pdb1igs/pdb |
関連するPDBエントリー | 1A53 1LBF 1LBL |
分子名称 | INDOLE-3-GLYCEROLPHOSPHATE SYNTHASE, PHOSPHATE ION (3 entities in total) |
機能のキーワード | thermostable, tim-barrel, synthase |
由来する生物種 | Sulfolobus solfataricus |
タンパク質・核酸の鎖数 | 1 |
化学式量合計 | 28721.07 |
構造登録者 | Hennig, M.,Darimont, B.,Kirschner, K.,Jansonius, J.N. (登録日: 1995-08-11, 公開日: 1996-07-11, 最終更新日: 2024-02-07) |
主引用文献 | Hennig, M.,Darimont, B.,Sterner, R.,Kirschner, K.,Jansonius, J.N. 2.0 A structure of indole-3-glycerol phosphate synthase from the hyperthermophile Sulfolobus solfataricus: possible determinants of protein stability. Structure, 3:1295-1306, 1995 Cited by PubMed Abstract: Recent efforts to understand the basis of protein stability have focused attention on comparative studies of proteins from hyperthermophilic and mesophilic organisms. Most work to date has been on either oligomeric enzymes or monomers comprising more than one domain. Such studies are hampered by the need to distinguish between stabilizing interactions acting between subunits or domains from those acting within domains. In order to simplify the search for determinants of protein stability we have chosen to study the monomeric enzyme indole-3-glycerol phosphate synthase from the hyperthermophilic archaeon Sulfolobus solfataricus (sIGPS), which grows optimally at 90 degrees C. PubMed: 8747456DOI: 10.1016/S0969-2126(01)00267-2 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2 Å) |
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