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4lgl

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{{STRUCTURE_4lgl| PDB=4lgl | SCENE= }}
{{STRUCTURE_4lgl| PDB=4lgl | SCENE= }}
===Crystal Structure of Glycine Decarboxylase P-protein from Synechocystis sp. PCC 6803, apo form===
===Crystal Structure of Glycine Decarboxylase P-protein from Synechocystis sp. PCC 6803, apo form===
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{{ABSTRACT_PUBMED_20124719}}
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{{ABSTRACT_PUBMED_24121504}}
==Function==
==Function==
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==Reference==
==Reference==
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<ref group="xtra">PMID:020124719</ref><references group="xtra"/><references/>
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<ref group="xtra">PMID:024121504</ref><references group="xtra"/><references/>
[[Category: Synechocystis sp. pcc 6803 substr. kazusa]]
[[Category: Synechocystis sp. pcc 6803 substr. kazusa]]
[[Category: Andersson, E.]]
[[Category: Andersson, E.]]

Revision as of 08:37, 30 October 2013

Template:STRUCTURE 4lgl

Contents

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

Template:ABSTRACT PUBMED 24121504

Function

[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 Structure

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

Reference

  • Hasse D, Andersson E, Carlsson G, Masloboy A, Hagemann M, Bauwe H, Andersson I. Structure of the Homodimeric Glycine Decarboxylase P-protein from Synechocystis sp. PCC 6803 Suggests a Mechanism for Redox-Regulation. J Biol Chem. 2013 Oct 11. PMID:24121504 doi:http://dx.doi.org/10.1074/jbc.M113.509976

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