4lhc: Difference between revisions
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{{STRUCTURE_4lhc| PDB=4lhc | SCENE= }} | {{STRUCTURE_4lhc| PDB=4lhc | SCENE= }} | ||
===Crystal structure of Synechocystis sp. PCC 6803 glycine decarboxylase (P-protein), holo form with pyridoxal-5'-phosphate and glycine=== | ===Crystal structure of Synechocystis sp. PCC 6803 glycine decarboxylase (P-protein), holo form with pyridoxal-5'-phosphate and glycine=== | ||
{{ | {{ABSTRACT_PUBMED_24121504}} | ||
==Function== | ==Function== | ||
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==Reference== | ==Reference== | ||
<ref group="xtra">PMID: | <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 11:46, 30 October 2013
Crystal structure of Synechocystis sp. PCC 6803 glycine decarboxylase (P-protein), holo form with pyridoxal-5'-phosphate and glycineCrystal structure of Synechocystis sp. PCC 6803 glycine decarboxylase (P-protein), holo form with pyridoxal-5'-phosphate and glycine
Template:ABSTRACT PUBMED 24121504
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
4lhc is a 2 chain structure with sequence from Synechocystis sp. pcc 6803 substr. kazusa. Full crystallographic information is available from OCA.
ReferenceReference
- ↑ 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