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TitleStructure of the Homodimeric Glycine Decarboxylase P-protein from Synechocystis sp. PCC 6803 Suggests a Mechanism for Redox Regulation.
Journal, issue, pagesJ. Biol. Chem., Vol. 288, Page 35333-35345, Year 2013
Publish dateJun 28, 2013 (structure data deposition date)
AuthorsHasse, D. / Andersson, E. / Carlsson, G. / Masloboy, A. / Hagemann, M. / Bauwe, H. / Andersson, I.
External linksJ. Biol. Chem. / PubMed:24121504
MethodsX-ray diffraction
Resolution1.7959 - 2.0004 Å
Structure data

PDB-4lgl:
Crystal Structure of Glycine Decarboxylase P-protein from Synechocystis sp. PCC 6803, apo form
Method: X-RAY DIFFRACTION / Resolution: 2.0004 Å

PDB-4lhc:
Crystal structure of Synechocystis sp. PCC 6803 glycine decarboxylase (P-protein), holo form with pyridoxal-5'-phosphate and glycine
Method: X-RAY DIFFRACTION / Resolution: 1.899 Å

PDB-4lhd:
Crystal structure of Synechocystis sp. PCC 6803 glycine decarboxylase (P-protein), holo form with pyridoxal-5'-phosphate and glycine, closed flexible loop
Method: X-RAY DIFFRACTION / Resolution: 1.7959 Å

Chemicals

ChemComp-TRS:
2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL / pH buffer*YM

ChemComp-CL:
Unknown entry

ChemComp-HOH:
WATER

ChemComp-GLY:
GLYCINE

ChemComp-BCT:
BICARBONATE ION / pH buffer*YM

ChemComp-PO4:
PHOSPHATE ION

ChemComp-EDO:
1,2-ETHANEDIOL

ChemComp-BCN:
BICINE / pH buffer*YM

Source
  • synechocystis sp. (bacteria)
KeywordsOXIDOREDUCTASE / alpha(2) homodimeric / dehydrogenase (decarboxylating) / S / S-(2-hydroxyethyl)thiocysteine / alpha(2) homodimer / cofactor pyridoxal 5'-phosphate

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