5MAP
X-ray generated oxyferrous complex of DtpA from Streptomyces lividans
5MAP の概要
| エントリーDOI | 10.2210/pdb5map/pdb |
| 分子名称 | DtpA, PROTOPORPHYRIN IX CONTAINING FE, OXYGEN MOLECULE, ... (4 entities in total) |
| 機能のキーワード | peroxidase radiolysis oxygen dye-type, oxidoreductase |
| 由来する生物種 | Streptomyces lividans TK24 |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 82345.51 |
| 構造登録者 | Moreno Chicano, T.,Chaplin, A.K.,Worrall, J.A.R.,Strange, R.W.,Hough, M.A. (登録日: 2016-11-04, 公開日: 2017-05-10, 最終更新日: 2024-01-17) |
| 主引用文献 | Kekilli, D.,Moreno-Chicano, T.,Chaplin, A.K.,Horrell, S.,Dworkowski, F.S.N.,Worrall, J.A.R.,Strange, R.W.,Hough, M.A. Photoreduction and validation of haem-ligand intermediate states in protein crystals by in situ single-crystal spectroscopy and diffraction. IUCrJ, 4:263-270, 2017 Cited by PubMed Abstract: Powerful synergies are available from the combination of multiple methods to study proteins in the crystalline form. Spectroscopies which probe the same region of the crystal from which X-ray crystal structures are determined can give insights into redox, ligand and spin states to complement the information gained from the electron-density maps. The correct assignment of crystal structures to the correct protein redox and ligand states is essential to avoid the misinterpretation of structural data. This is a particular concern for haem proteins, which can occupy a wide range of redox states and are exquisitely sensitive to becoming reduced by solvated electrons generated from interactions of X-rays with water molecules in the crystal. Here, single-crystal spectroscopic fingerprinting has been applied to investigate the laser photoreduction of ferric haem in cytochrome '. Furthermore, X-ray-driven generation of haem intermediates in crystals of the dye-decolourizing-type peroxidase A (DtpA) from is described. PubMed: 28512573DOI: 10.1107/S2052252517002159 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.49 Å) |
構造検証レポート
検証レポート(詳細版)
をダウンロード






