1t0i
From Proteopedia
(New page: 200px<br /><applet load="1t0i" size="450" color="white" frame="true" align="right" spinBox="true" caption="1t0i, resolution 2.00Å" /> '''YLR011wp, a Saccharo...) |
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| - | [[Image:1t0i.jpg|left|200px]]<br /><applet load="1t0i" size=" | + | [[Image:1t0i.jpg|left|200px]]<br /><applet load="1t0i" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1t0i, resolution 2.00Å" /> | caption="1t0i, resolution 2.00Å" /> | ||
'''YLR011wp, a Saccharomyces cerevisiae NA(D)PH-dependent FMN reductase'''<br /> | '''YLR011wp, a Saccharomyces cerevisiae NA(D)PH-dependent FMN reductase'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Flavodoxins are involved in a variety of electron transfer reactions that | + | 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. |
==About this Structure== | ==About this Structure== | ||
| - | 1T0I is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with CA and FMN as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1T0I is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=FMN:'>FMN</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1T0I OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Liger, D.]] | [[Category: Liger, D.]] | ||
[[Category: Quevillon-Cheruel, S.]] | [[Category: Quevillon-Cheruel, S.]] | ||
| - | [[Category: Tilbeurgh, H | + | [[Category: Tilbeurgh, H van.]] |
| - | [[Category: Zhou, C | + | [[Category: Zhou, C Z.]] |
[[Category: CA]] | [[Category: CA]] | ||
[[Category: FMN]] | [[Category: FMN]] | ||
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[[Category: saccharomyces cerevisiae]] | [[Category: saccharomyces cerevisiae]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:08:31 2008'' |
Revision as of 13:08, 21 February 2008
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YLR011wp, a Saccharomyces cerevisiae NA(D)PH-dependent FMN reductase
Overview
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.
About this Structure
1T0I is a Single protein structure of sequence from Saccharomyces cerevisiae with and as ligands. Full crystallographic information is available from OCA.
Reference
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
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