1T0I
YLR011wp, a Saccharomyces cerevisiae NA(D)PH-dependent FMN reductase
1T0I の概要
| エントリーDOI | 10.2210/pdb1t0i/pdb |
| 関連するPDBエントリー | 1NNI |
| 分子名称 | YLR011wp, CALCIUM ION, FLAVIN MONONUCLEOTIDE, ... (4 entities in total) |
| 機能のキーワード | saccharomyces cerevisiae, fmn binding protein, flavodoxin, azoreductase, oxidoreductase |
| 由来する生物種 | Saccharomyces cerevisiae (baker's yeast) |
| 細胞内の位置 | Cytoplasm: Q07923 |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 43603.96 |
| 構造登録者 | Liger, D.,Graille, M.,Zhou, C.-Z.,Leulliot, N.,Quevillon-Cheruel, S.,Blondeau, K.,Janin, J.,van Tilbeurgh, H. (登録日: 2004-04-09, 公開日: 2004-06-22, 最終更新日: 2024-02-14) |
| 主引用文献 | Liger, D.,Graille, M.,Zhou, C.-Z.,Leulliot, N.,Quevillon-Cheruel, S.,Blondeau, K.,Janin, J.,Van Tilbeurgh, H. Crystal Structure and Functional Characterization of Yeast YLR011wp, an Enzyme with NAD(P)H-FMN and Ferric Iron Reductase Activities J.Biol.Chem., 279:34890-34897, 2004 Cited by PubMed Abstract: Flavodoxins are involved in a variety of electron transfer reactions that are essential for life. Although FMN-binding proteins are well characterized in prokaryotic organisms, information is scarce for eukaryotic flavodoxins. We describe the 2.0-A resolution crystal structure of the Saccharomyces cerevisiae YLR011w gene product, a predicted flavoprotein. YLR011wp indeed adopts a flavodoxin fold, binds the FMN cofactor, and self-associates as a homodimer. Despite the absence of the flavodoxin key fingerprint motif involved in FMN binding, YLR011wp binds this cofactor in a manner very analogous to classical flavodoxins. YLR011wp closest structural homologue is the homodimeric Bacillus subtilis Yhda protein (25% sequence identity) whose homodimer perfectly superimposes onto the YLR011wp one. Yhda, whose function is not documented, has 53% sequence identity with the Bacillus sp. OY1-2 azoreductase. We show that YLR011wp has an NAD(P)H-dependent FMN reductase and a strong ferricyanide reductase activity. We further demonstrate a weak but specific reductive activity on azo dyes and nitrocompounds. PubMed: 15184374DOI: 10.1074/jbc.M405404200 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2 Å) |
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