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PDBsum entry 2rgo
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Oxidoreductase
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PDB id
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2rgo
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References listed in PDB file
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Key reference
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Title
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Structure of alpha-Glycerophosphate oxidase from streptococcus sp.: A template for the mitochondrial alpha-Glycerophosphate dehydrogenase.
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Authors
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T.Colussi,
D.Parsonage,
W.Boles,
T.Matsuoka,
T.C.Mallett,
P.A.Karplus,
A.Claiborne.
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Ref.
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Biochemistry, 2008,
47,
965-977.
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PubMed id
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Abstract
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The FAD-dependent alpha-glycerophosphate oxidase (GlpO) from Enterococcus
casseliflavus and Streptococcus sp. was originally studied as a soluble
flavoprotein oxidase; surprisingly, the GlpO sequence is 30-43% identical to
those of the alpha-glycerophosphate dehydrogenases (GlpDs) from mitochondrial
and bacterial sources. The structure of a deletion mutant of Streptococcus sp.
GlpO (GlpODelta, lacking a 50-residue insert that includes a flexible surface
region) has been determined using multiwavelength anomalous dispersion data and
refined at 2.3 A resolution. Using the GlpODelta structure as a search model, we
have also determined the intact GlpO structure, as refined at 2.4 A resolution.
The first two domains of the GlpO fold are most closely related to those of the
flavoprotein glycine oxidase, where they function in FAD binding and substrate
binding, respectively; the GlpO C-terminal domain consists of two helix bundles
and is not closely related to any known structure. The flexible surface region
in intact GlpO corresponds to a segment of missing electron density that links
the substrate-binding domain to a betabetaalpha element of the FAD-binding
domain. In accordance with earlier biochemical studies (stabilizations of the
covalent FAD-N5-sulfite adduct and p-quinonoid form of 8-mercapto-FAD),
Ile430-N, Thr431-N, and Thr431-OG are hydrogen bonded to FAD-O2alpha in
GlpODelta, stabilizing the negative charge in these two modified flavins and
facilitating transfer of a hydride to FAD-N5 (from Glp) as well. Active-site
overlays with the glycine oxidase-N-acetylglycine and d-amino acid
oxidase-d-alanine complexes demonstrate that Arg346 of GlpODelta is structurally
equivalent to Arg302 and Arg285, respectively; in both cases, these residues
interact directly with the amino acid substrate or inhibitor carboxylate. The
structural and functional divergence between GlpO and the bacterial and
mitochondrial GlpDs is also discussed.
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