1oyb: Difference between revisions
New page: left|200px<br /><applet load="1oyb" size="450" color="white" frame="true" align="right" spinBox="true" caption="1oyb, resolution 2.0Å" /> '''OLD YELLOW ENZYME AT ... |
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[[Image:1oyb.jpg|left|200px]]<br /><applet load="1oyb" size=" | [[Image:1oyb.jpg|left|200px]]<br /><applet load="1oyb" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1oyb, resolution 2.0Å" /> | caption="1oyb, resolution 2.0Å" /> | ||
'''OLD YELLOW ENZYME AT 2 ANGSTROMS RESOLUTION: OVERALL STRUCTURE, LIGAND BINDING AND COMPARISON WITH RELATED FLAVOPROTEINS'''<br /> | '''OLD YELLOW ENZYME AT 2 ANGSTROMS RESOLUTION: OVERALL STRUCTURE, LIGAND BINDING AND COMPARISON WITH RELATED FLAVOPROTEINS'''<br /> | ||
==Overview== | ==Overview== | ||
BACKGROUND: Old yellow enzyme (OYE) was the first flavoenzyme purified, but its function is still unknown. Nevertheless, the NADPH oxidase | BACKGROUND: Old yellow enzyme (OYE) was the first flavoenzyme purified, but its function is still unknown. Nevertheless, the NADPH oxidase activity, the flavin mononucleotide environment and the ligand-binding properties of OYE have been extensively studied by biochemical and spectroscopic approaches. Full interpretation of these data requires structural information. RESULTS: The crystal structures of oxidized and reduced OYE at 2 A resolution reveal an alpha/beta-barrel topology clearly related to trimethylamine dehydrogenase. Complexes of OYE with p-hydroxybenzaldehyde, beta-estradiol, and an NADPH analog show all three binding at a common site, stacked on the flavin. The putative NADPH binding mode is novel as it involves primary recognition of the nicotinamide mononucleotide portion. CONCLUSIONS: This work shows that the striking spectral changes seen upon phenol binding are due to close physical association of the flavin and phenolate. It also identifies the structural class of OYE and suggests that if NADPH is its true substrate, then OYE has adopted NADPH dependence during evolution. | ||
==About this Structure== | ==About this Structure== | ||
1OYB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_pastorianus Saccharomyces pastorianus] with FMN and HBA as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/NADPH_dehydrogenase NADPH dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.6.99.1 1.6.99.1] Full crystallographic information is available from [http:// | 1OYB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_pastorianus Saccharomyces pastorianus] with <scene name='pdbligand=FMN:'>FMN</scene> and <scene name='pdbligand=HBA:'>HBA</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/NADPH_dehydrogenase NADPH dehydrogenase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=1.6.99.1 1.6.99.1] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OYB OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Saccharomyces pastorianus]] | [[Category: Saccharomyces pastorianus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Fox, K | [[Category: Fox, K M.]] | ||
[[Category: Karplus, P | [[Category: Karplus, P A.]] | ||
[[Category: FMN]] | [[Category: FMN]] | ||
[[Category: HBA]] | [[Category: HBA]] | ||
[[Category: oxidoreductase(flavoprotein)]] | [[Category: oxidoreductase(flavoprotein)]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:23:06 2008'' | ||
Revision as of 15:23, 21 February 2008
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OLD YELLOW ENZYME AT 2 ANGSTROMS RESOLUTION: OVERALL STRUCTURE, LIGAND BINDING AND COMPARISON WITH RELATED FLAVOPROTEINS
OverviewOverview
BACKGROUND: Old yellow enzyme (OYE) was the first flavoenzyme purified, but its function is still unknown. Nevertheless, the NADPH oxidase activity, the flavin mononucleotide environment and the ligand-binding properties of OYE have been extensively studied by biochemical and spectroscopic approaches. Full interpretation of these data requires structural information. RESULTS: The crystal structures of oxidized and reduced OYE at 2 A resolution reveal an alpha/beta-barrel topology clearly related to trimethylamine dehydrogenase. Complexes of OYE with p-hydroxybenzaldehyde, beta-estradiol, and an NADPH analog show all three binding at a common site, stacked on the flavin. The putative NADPH binding mode is novel as it involves primary recognition of the nicotinamide mononucleotide portion. CONCLUSIONS: This work shows that the striking spectral changes seen upon phenol binding are due to close physical association of the flavin and phenolate. It also identifies the structural class of OYE and suggests that if NADPH is its true substrate, then OYE has adopted NADPH dependence during evolution.
About this StructureAbout this Structure
1OYB is a Single protein structure of sequence from Saccharomyces pastorianus with and as ligands. Active as NADPH dehydrogenase, with EC number 1.6.99.1 Full crystallographic information is available from OCA.
ReferenceReference
Old yellow enzyme at 2 A resolution: overall structure, ligand binding, and comparison with related flavoproteins., Fox KM, Karplus PA, Structure. 1994 Nov 15;2(11):1089-105. PMID:7881908
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