3N38
Ribonucleotide Reductase NrdF from Escherichia coli Soaked with Ferrous Ions
3N38 の概要
エントリーDOI | 10.2210/pdb3n38/pdb |
関連するPDBエントリー | 3N37 3N39 3N3A 3N3B |
分子名称 | Ribonucleoside-diphosphate reductase 2 subunit beta, FE (II) ION (3 entities in total) |
機能のキーワード | ribonucleotide reductase, four-helix bundle, diferrous cluster, oxidoreductase |
由来する生物種 | Escherichia coli |
タンパク質・核酸の鎖数 | 1 |
化学式量合計 | 36586.76 |
構造登録者 | Boal, A.K.,Cotruvo Jr., J.A.,Stubbe, J.,Rosenzweig, A.C. (登録日: 2010-05-19, 公開日: 2010-08-18, 最終更新日: 2023-09-06) |
主引用文献 | Boal, A.K.,Cotruvo, J.A.,Stubbe, J.,Rosenzweig, A.C. Structural basis for activation of class Ib ribonucleotide reductase. Science, 329:1526-1530, 2010 Cited by PubMed Abstract: The class Ib ribonucleotide reductase of Escherichia coli can initiate reduction of nucleotides to deoxynucleotides with either a Mn(III)2-tyrosyl radical (Y•) or a Fe(III)2-Y• cofactor in the NrdF subunit. Whereas Fe(III)2-Y• can self-assemble from Fe(II)2-NrdF and O2, activation of Mn(II)2-NrdF requires a reduced flavoprotein, NrdI, proposed to form the oxidant for cofactor assembly by reduction of O2. The crystal structures reported here of E. coli Mn(II)2-NrdF and Fe(II)2-NrdF reveal different coordination environments, suggesting distinct initial binding sites for the oxidants during cofactor activation. In the structures of Mn(II)2-NrdF in complex with reduced and oxidized NrdI, a continuous channel connects the NrdI flavin cofactor to the NrdF Mn(II)2 active site. Crystallographic detection of a putative peroxide in this channel supports the proposed mechanism of Mn(III)2-Y• cofactor assembly. PubMed: 20688982DOI: 10.1126/science.1190187 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (1.9 Å) |
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