1t0i | pdb_00001t0i

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

spinqualitylabelsall models 1t0i, resolution 2.00Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1t0i is a 2 chain structure with sequence from Atcc 18824. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CA, FMN Related: 1nni Gene: YLR011w (ATCC 18824) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [LOT6_YEAST] Has several reductase activities that are NAD(P)H-dependent and involve FMN as a cofactor, ferricyanide being the best substrate for reduction. May be involved in ferric iron assimilation. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed 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. Crystal structure and functional characterization of yeast YLR011wp, an enzyme with NAD(P)H-FMN and ferric iron reductase activities.,Liger D, Graille M, Zhou CZ, Leulliot N, Quevillon-Cheruel S, Blondeau K, Janin J, van Tilbeurgh H J Biol Chem. 2004 Aug 13;279(33):34890-7. Epub 2004 Jun 7. PMID:15184374 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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