1JNR
Structure of adenylylsulfate reductase from the hyperthermophilic Archaeoglobus fulgidus at 1.6 resolution
1JNR の概要
| エントリーDOI | 10.2210/pdb1jnr/pdb |
| 分子名称 | adenylylsulfate reductase, FLAVIN-ADENINE DINUCLEOTIDE, GLYCEROL, ... (6 entities in total) |
| 機能のキーワード | sulfur metabolism/ adenylylsulfate reductase/ iron-sulfur flavoprotein/ crystal structure/catalysis, oxidoreductase |
| 由来する生物種 | Archaeoglobus fulgidus DSM 4304 詳細 |
| タンパク質・核酸の鎖数 | 4 |
| 化学式量合計 | 183950.57 |
| 構造登録者 | Fritz, G.,Roth, A.,Schiffer, A.,Buechert, T.,Bourenkov, G.,Bartunik, H.D.,Huber, H.,Stetter, K.O.,Kroneck, P.M.H.,Ermler, U. (登録日: 2001-07-25, 公開日: 2002-02-27, 最終更新日: 2024-02-07) |
| 主引用文献 | Fritz, G.,Roth, A.,Schiffer, A.,Buchert, T.,Bourenkov, G.,Bartunik, H.D.,Huber, H.,Stetter, K.O.,Kroneck, P.M.,Ermler, U. Structure of adenylylsulfate reductase from the hyperthermophilic Archaeoglobus fulgidus at 1.6-A resolution Proc.Natl.Acad.Sci.USA, 99:1836-1841, 2002 Cited by PubMed Abstract: The iron-sulfur flavoenzyme adenylylsulfate (adenosine 5'-phosphosulfate, APS) reductase catalyzes reversibly the reduction of APS to sulfite and AMP. The structures of APS reductase from the hyperthermophilic Archaeoglobus fulgidus in the two-electron reduced state and with sulfite bound to FAD are reported at 1.6- and 2.5- resolution, respectively. The FAD-sulfite adduct was detected after soaking the crystals with APS. This finding and the architecture of the active site strongly suggest that catalysis involves a nucleophilic attack of the N5 atom of reduced FAD on the sulfur atom of APS. In view of the high degree of similarity between APS reductase and fumarate reductase especially with regard to the FAD-binding alpha-subunit, it is proposed that both subunits originate from a common ancestor resembling archaeal APS reductase. The two electrons required for APS reduction are transferred via two [4Fe-4S] clusters from the surface of the protein to FAD. The exceptionally large difference in reduction potential of these clusters (-60 and -500 mV) can be explained by interactions of the clusters with the protein matrix. PubMed: 11842205DOI: 10.1073/pnas.042664399 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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