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PDBsum entry 4lhc
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Oxidoreductase
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PDB id
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4lhc
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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 the homodimeric glycine decarboxylase p-Protein from synechocystis sp. Pcc 6803 suggests a mechanism for redox regulation.
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Authors
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D.Hasse,
E.Andersson,
G.Carlsson,
A.Masloboy,
M.Hagemann,
H.Bauwe,
I.Andersson.
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Ref.
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J Biol Chem, 2013,
288,
35333-35345.
[DOI no: ]
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PubMed id
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Abstract
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Glycine decarboxylase, or P-protein, is a pyridoxal 5'-phosphate (PLP)-dependent
enzyme in one-carbon metabolism of all organisms, in the glycine and serine
catabolism of vertebrates, and in the photorespiratory pathway of oxygenic
phototrophs. P-protein from the cyanobacterium Synechocystis sp. PCC 6803 is an
α2 homodimer with high homology to eukaryotic P-proteins. The crystal structure
of the apoenzyme shows the C terminus locked in a closed conformation by a
disulfide bond between Cys(972) in the C terminus and Cys(353) located in the
active site. The presence of the disulfide bridge isolates the active site from
solvent and hinders the binding of PLP and glycine in the active site. Variants
produced by substitution of Cys(972) and Cys(353) by Ser using site-directed
mutagenesis have distinctly lower specific activities, supporting the crucial
role of these highly conserved redox-sensitive amino acid residues for P-protein
activity. Reduction of the 353-972 disulfide releases the C terminus and allows
access to the active site. PLP and the substrate glycine bind in the active site
of this reduced enzyme and appear to cause further conformational changes
involving a flexible surface loop. The observation of the disulfide bond that
acts to stabilize the closed form suggests a molecular mechanism for the
redox-dependent activation of glycine decarboxylase observed earlier.
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Secondary reference #1
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Title
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Crystallization and preliminary X-Ray diffraction analyses of the homodimeric glycine decarboxylase (p-Protein) from the cyanobacterium synechocystis sp. Pcc 6803.
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Authors
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D.Hasse,
M.Hagemann,
I.Andersson,
H.Bauwe.
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Ref.
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Acta Crystallogr Sect F Struct Biol Cryst Commun, 2010,
66,
187-191.
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PubMed id
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