1t0i

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[[Image:1t0i.jpg|left|200px]]
[[Image:1t0i.jpg|left|200px]]
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{{Structure
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<!--
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|PDB= 1t0i |SIZE=350|CAPTION= <scene name='initialview01'>1t0i</scene>, resolution 2.00&Aring;
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The line below this paragraph, containing "STRUCTURE_1t0i", creates the "Structure Box" on the page.
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|SITE=
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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|ACTIVITY=
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or leave the SCENE parameter empty for the default display.
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|GENE= YLR011w ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae])
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|DOMAIN=
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{{STRUCTURE_1t0i| PDB=1t0i | SCENE= }}
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|RELATEDENTRY=[[1nni|1NNI]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1t0i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1t0i OCA], [http://www.ebi.ac.uk/pdbsum/1t0i PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1t0i RCSB]</span>
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}}
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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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[[Category: Tilbeurgh, H van.]]
[[Category: Tilbeurgh, H van.]]
[[Category: Zhou, C Z.]]
[[Category: Zhou, C Z.]]
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[[Category: azoreductase]]
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[[Category: Azoreductase]]
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[[Category: flavodoxin]]
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[[Category: Flavodoxin]]
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[[Category: fmn binding protein]]
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[[Category: Fmn binding protein]]
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[[Category: saccharomyces cerevisiae]]
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[[Category: Saccharomyces cerevisiae]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 09:21:10 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:49:30 2008''
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Revision as of 06:21, 3 May 2008

Template:STRUCTURE 1t0i

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. 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 Page seeded by OCA on Sat May 3 09:21:10 2008

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