1IO8
Thermophilic cytochrome P450 (CYP119) from sulfolobus solfataricus: High resolution structural origin of its thermostability and functional properties
1IO8 の概要
エントリーDOI | 10.2210/pdb1io8/pdb |
関連するPDBエントリー | 1IO7 1IO9 |
分子名称 | CYTOCHROME P450 CYP119, PROTOPORPHYRIN IX CONTAINING FE (3 entities in total) |
機能のキーワード | thermophilic, cytochromo p450, riken structural genomics/proteomics initiative, rsgi, structural genomics, oxidoreductase, nppsfa, national project on protein structural and functional analyses |
由来する生物種 | Sulfolobus solfataricus |
細胞内の位置 | Cytoplasm (Probable): Q55080 |
タンパク質・核酸の鎖数 | 2 |
化学式量合計 | 87013.00 |
構造登録者 | Park, S.-Y.,Yamane, K.,Adachi, S.,Shiro, Y.,Sligar, S.G.,RIKEN Structural Genomics/Proteomics Initiative (RSGI) (登録日: 2001-02-08, 公開日: 2001-03-07, 最終更新日: 2024-04-03) |
主引用文献 | Park, S.Y.,Yamane, K.,Adachi, S.,Shiro, Y.,Weiss, K.E.,Maves, S.A.,Sligar, S.G. Thermophilic cytochrome P450 (CYP119) from Sulfolobus solfataricus: high resolution structure and functional properties J.Inorg.Biochem., 91:491-501, 2002 Cited by PubMed Abstract: Crystal structures of a thermostable cytochrome P450 (CYP119) and a site-directed mutant, (Phe24Leu), from the acidothermophilic archaea Sulfolobus solfataricus were determined at 1.5-2.0 A resolution. We identify important crystallographic waters in the ferric heme pocket, observe protein conformational changes upon inhibitor binding, and detect a unique distribution of surface charge not found in other P450s. An analysis of factors contributing to thermostability of CYP119 of these high resolution structures shows an apparent increase in clustering of aromatic residues and optimum stacking. The contribution of aromatic stacking was investigated further with the mutant crystal structure and differential scanning calorimetry. PubMed: 12237217DOI: 10.1107/S0907444900008234 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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