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1T0I

YLR011wp, a Saccharomyces cerevisiae NA(D)PH-dependent FMN reductase

1T0I の概要
エントリーDOI10.2210/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: 15184374
DOI: 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)
構造検証レポート
Validation report summary of 1t0i
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2026-04-22に公開中

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