1T0I

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

Summary for 1T0I

• Entry DOI: 10.2210/pdb1t0i/pdb
• Related: 1NNI
• Descriptor: YLR011wp, CALCIUM ION, FLAVIN MONONUCLEOTIDE, ... (4 entities in total)
• Functional Keywords: saccharomyces cerevisiae, fmn binding protein, flavodoxin, azoreductase, oxidoreductase
• Biological source: Saccharomyces cerevisiae (baker's yeast)
• Cellular location: Cytoplasm: Q07923
• Total number of polymer chains: 2
• Total formula weight: 43603.96

Authors

Liger, D.,Graille, M.,Zhou, C.-Z.,Leulliot, N.,Quevillon-Cheruel, S.,Blondeau, K.,Janin, J.,van Tilbeurgh, H. (deposition date: 2004-04-09, release date: 2004-06-22, Last modification date: 2024-02-14)

Primary citation

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

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

Experimental method

X-RAY DIFFRACTION (2 Å)