3EXB
Crystal structure of Cytochrome C Peroxidase with a Proposed Electron Pathway Excised in a Complex with a Peptide Wire
3EXB の概要
| エントリーDOI | 10.2210/pdb3exb/pdb |
| 関連するPDBエントリー | 1KXM 1KXN |
| 関連するBIRD辞書のPRD_ID | PRD_000453 |
| 分子名称 | Cytochrome c peroxidase, N-[3-(1H-BENZIMIDAZOL-1-YL)PROPANOYL]GLYCYL-L-ALANYL-L-ALANINAMIDE, PROTOPORPHYRIN IX CONTAINING FE, ... (4 entities in total) |
| 機能のキーワード | oxidoreductase, peroxidase, heme, hydrogen peroxide, iron, metal-binding, mitochondrion, transit peptide, oxidoreductase-peptide complex, oxidoreductase/peptide |
| 由来する生物種 | Saccharomyces cerevisiae (Baker's yeast) 詳細 |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 34593.28 |
| 構造登録者 | |
| 主引用文献 | Hays Putnam, A.M.,Lee, Y.T.,Goodin, D.B. Replacement of an electron transfer pathway in cytochrome c peroxidase with a surrogate peptide Biochemistry, 48:1-3, 2009 Cited by PubMed Abstract: A proposed electron transfer pathway in cytochrome c peroxidase was previously excised from the structure by design. The engineered channel mutant was shown to bind peptide surrogates without restoration of cyt c oxidation. Here, we report the 1.6 A crystal structure of (N-benzimidazole-propionic acid)-Gly-Ala-Ala bound within the engineered channel. The peptide retains many features of the native electron transfer pathway: placement of benzimidazole at the position of the Trp-191 radical, hydrogen bonding to Asp235, and positioning of the C-terminus near the point where wild type CcP makes closest contact to cyt c. The inability of this surrogate pathway to restore function supports proposals that electron transfer requires the Trp-191 radical. PubMed: 19072042DOI: 10.1021/bi8020263 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.6 Å) |
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