1F4U
THERMOPHILIC P450: CYP119 FROM SULFOLOBUS SOLFACTARICUS
1F4U の概要
| エントリーDOI | 10.2210/pdb1f4u/pdb |
| 関連するPDBエントリー | 1F4T |
| 分子名称 | CYTOCHROME P450 119, SULFATE ION, PROTOPORPHYRIN IX CONTAINING FE, ... (5 entities in total) |
| 機能のキーワード | p450 fold, oxidoreductase |
| 由来する生物種 | Sulfolobus solfataricus |
| 細胞内の位置 | Cytoplasm : Q55080 |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 87411.32 |
| 構造登録者 | Yano, J.K.,Koo, L.S.,Schuller, D.J.,Li, H.,Ortiz de Montellano, P.R.,Poulos, T.L. (登録日: 2000-06-09, 公開日: 2000-10-23, 最終更新日: 2024-02-07) |
| 主引用文献 | Yano, J.K.,Koo, L.S.,Schuller, D.J.,Li, H.,Ortiz de Montellano, P.R.,Poulos, T.L. Crystal structure of a thermophilic cytochrome P450 from the archaeon Sulfolobus solfataricus. J.Biol.Chem., 275:31086-31092, 2000 Cited by PubMed Abstract: The structure of the first P450 identified in Archaea, CYP119 from Sulfolobus solfataricus, has been solved in two different crystal forms that differ by the ligand (imidazole or 4-phenylimidazole) coordinated to the heme iron. A comparison of the two structures reveals an unprecedented rearrangement of the active site to adapt to the different size and shape of ligands bound to the heme iron. These changes involve unraveling of the F helix C-terminal segment to extend a loop structure connecting the F and G helices, allowing the longer loop to dip down into the active site and interact with the smaller imidazole ligand. A comparison of CYP119 with P450cam and P450eryF indicates an extensive clustering of aromatic residues may provide the structural basis for the enhanced thermal stability of CYP119. An additional feature of the 4-phenylimidazole-bound structure is a zinc ion tetrahedrally bound by symmetry-related His and Glu residues. PubMed: 10859321DOI: 10.1074/jbc.M004281200 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.69 Å) |
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