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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DOI10.2210/pdb3exb/pdb
関連するPDBエントリー1KXM 1KXN
関連するBIRD辞書のPRD_IDPRD_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
Putnam, A.-M.A.,Lee, Y.-T.,Goodin, D.B. (登録日: 2008-10-16, 公開日: 2009-01-13, 最終更新日: 2024-10-16)
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: 19072042
DOI: 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)
構造検証レポート
Validation report summary of 3exb
検証レポート(詳細版)ダウンロードをダウンロード

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件を2025-12-31に公開中

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