1t0i
From Proteopedia
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|PDB= 1t0i |SIZE=350|CAPTION= <scene name='initialview01'>1t0i</scene>, resolution 2.00Å | |PDB= 1t0i |SIZE=350|CAPTION= <scene name='initialview01'>1t0i</scene>, resolution 2.00Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> | + | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=FMN:FLAVIN+MONONUCLEOTIDE'>FMN</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= YLR011w ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae]) | |GENE= YLR011w ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1nni|1NNI]] | ||
| + | |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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[[Category: Tilbeurgh, H van.]] | [[Category: Tilbeurgh, H van.]] | ||
[[Category: Zhou, C Z.]] | [[Category: Zhou, C Z.]] | ||
| - | [[Category: CA]] | ||
| - | [[Category: FMN]] | ||
[[Category: azoreductase]] | [[Category: azoreductase]] | ||
[[Category: flavodoxin]] | [[Category: flavodoxin]] | ||
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[[Category: saccharomyces cerevisiae]] | [[Category: saccharomyces cerevisiae]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:49:30 2008'' |
Revision as of 20:49, 30 March 2008
| |||||||
| , resolution 2.00Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Gene: | YLR011w (Saccharomyces cerevisiae) | ||||||
| Related: | 1NNI
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
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