4lgl

Crystal Structure of Glycine Decarboxylase P-protein from Synechocystis sp. PCC 6803, apo formCrystal Structure of Glycine Decarboxylase P-protein from Synechocystis sp. PCC 6803, apo form

Template:ABSTRACT PUBMED 20124719

FunctionFunction

[GCSP_SYNY3] The glycine cleavage system catalyzes the degradation of glycine. The P protein binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein (By similarity).

About this StructureAbout this Structure

4lgl is a 2 chain structure with sequence from Synechocystis sp. pcc 6803 substr. kazusa. Full crystallographic information is available from OCA.

ReferenceReference

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↑ Hasse D, Hagemann M, Andersson I, Bauwe H. Crystallization and preliminary X-ray diffraction analyses of the homodimeric glycine decarboxylase (P-protein) from the cyanobacterium Synechocystis sp. PCC 6803. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Feb 1;66(Pt 2):187-91., doi: 10.1107/S1744309109052828. Epub 2010 Jan 28. PMID:20124719 doi:http://dx.doi.org/10.1107/S1744309109052828

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OCA

[1] Hasse D, Hagemann M, Andersson I, Bauwe H. Crystallization and preliminary X-ray diffraction analyses of the homodimeric glycine decarboxylase (P-protein) from the cyanobacterium Synechocystis sp. PCC 6803. Acta Crystallogr Sect F Struct Biol Cryst Commun. 2010 Feb 1;66(Pt 2):187-91., doi: 10.1107/S1744309109052828. Epub 2010 Jan 28. PMID:20124719 doi:http://dx.doi.org/10.1107/S1744309109052828

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