1D3S
1.4 A crystal structure of nitrophorin 4 from Rhodnius prolixis at pH=5.6.
1D3S の概要
| エントリーDOI | 10.2210/pdb1d3s/pdb |
| 関連するPDBエントリー | 1D2U 1NP4 |
| 分子名称 | NITROPHORIN 4, PROTOPORPHYRIN IX CONTAINING FE (3 entities in total) |
| 機能のキーワード | nitric oxide transport, ferric heme, antihistamine, vasodilator, lipocalin, transport protein |
| 由来する生物種 | Rhodnius prolixus |
| 細胞内の位置 | Secreted: Q94734 |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 20909.15 |
| 構造登録者 | Weichsel, A.,Andersen, J.F.,Roberts, S.A.,Montfort, W.R. (登録日: 1999-09-30, 公開日: 2000-07-07, 最終更新日: 2024-10-30) |
| 主引用文献 | Weichsel, A.,Andersen, J.F.,Roberts, S.A.,Montfort, W.R. Nitric oxide binding to nitrophorin 4 induces complete distal pocket burial. Nat.Struct.Biol., 7:551-554, 2000 Cited by PubMed Abstract: The nitrophorins comprise an unusual family of proteins that use ferric (Fe(III)) heme to transport highly reactive nitric oxide (NO) from the salivary gland of a blood sucking bug to the victim, resulting in vasodilation and reduced blood coagulation. We have determined structures of nitrophorin 4 in complexes with H2O, cyanide and nitric oxide. These structures reveal a remarkable feature: the nitrophorins have a broadly open distal pocket in the absence of NO, but upon NO binding, three or more water molecules are expelled and two loops fold into the distal pocket, resulting in the packing of hydrophobic groups around the NO molecule and increased distortion of the heme. In this way, the protein apparently forms a 'hydrophobic trap' for the NO molecule. The structures are very accurate, ranging between 1.6 and 1.4 A resolutions. PubMed: 10876239DOI: 10.1038/76769 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.4 Å) |
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