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| {{STRUCTURE_1t0i| PDB=1t0i | SCENE= }} | | {{STRUCTURE_1t0i| PDB=1t0i | SCENE= }} |
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| '''YLR011wp, a Saccharomyces cerevisiae NA(D)PH-dependent FMN reductase'''
| | ===YLR011wp, a Saccharomyces cerevisiae NA(D)PH-dependent FMN reductase=== |
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| ==Overview==
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| 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.
| | The line below this paragraph, {{ABSTRACT_PUBMED_15184374}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 15184374 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_15184374}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Fmn binding protein]] | | [[Category: Fmn binding protein]] |
| [[Category: Saccharomyces cerevisiae]] | | [[Category: Saccharomyces cerevisiae]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 09:21:10 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 17:58:27 2008'' |
