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PDBsum entry 1oyc
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Oxidoreductase(flavoprotein)
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PDB id
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1oyc
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References listed in PDB file
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Key reference
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Title
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Old yellow enzyme at 2 a resolution: overall structure, Ligand binding, And comparison with related flavoproteins.
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Authors
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K.M.Fox,
P.A.Karplus.
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Ref.
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Structure, 1994,
2,
1089-1105.
[DOI no: ]
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PubMed id
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Abstract
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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.
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Figure 13.
Figure 13. Comparison of PHB, BED and (c–THN)TPN binding.
Shown are FMN, His191 and Asn194 from the native structure
(yellow) overlayed with the bound conformations of PHB (green),
BED (red) and the ordered portion of (c–THN)TPN (violet).
Arrows indicate the two hydrogen bonds donated to ligand oxygens
which appear to be major determinants of binding. Figure
13. Comparison of PHB, BED and (c–THN)TPN binding. Shown are
FMN, His191 and Asn194 from the native structure (yellow)
overlayed with the bound conformations of PHB (green), BED (red)
and the ordered portion of (c–THN)TPN (violet). Arrows
indicate the two hydrogen bonds donated to ligand oxygens which
appear to be major determinants of binding.
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Figure 15.
Figure 15. Comparison of FMN in the oxidized (yellow) and
reduced (green) states. The refined structures are shown for
FMN, His191 and Asn194. Two preferred water sites seen in the
reduced state are also included. Difference electron density is
shown contoured at +4.0 ρ[rms] (violet) and –4.0 ρ[rms]
(red). The large negative peak reflects the loss of the chloride
ion. Figure 15. Comparison of FMN in the oxidized (yellow)
and reduced (green) states. The refined structures are shown for
FMN, His191 and Asn194. Two preferred water sites seen in the
reduced state are also included. Difference electron density is
shown contoured at +4.0 ρ[rms] (violet) and –4.0 ρ[rms]
(red). The large negative peak reflects the loss of the chloride
ion.
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The above figures are
reprinted
by permission from Cell Press:
Structure
(1994,
2,
1089-1105)
copyright 1994.
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