Crystallographic data for H-protein from the glycine decarboxylase complex.
The H-protein is the pivotal enzyme of the glycine decarboxylase complex responsible for the oxidation of glycine by mitochondria. It has been extracted and purified from pea leaf mitochondria (Pisum sativum). Its molecular weight, based on the amino acid sequence, is 13.3 kDa and it crystallizes in the space group P3(1)21 (or its enantiomorph P3(2)21) with a = b = 57.14 (3) A, c = 137.11 (11) A. The crystals diffract until at least 3.5 A resolution.
Sieker
L
L
CNRS, URA 1333, Centre d'Etudes Nucléaires, Grenoble, France.
Cohen-Addad
C
C
Neuburger
M
M
Douce
R
R
D000594:Amino Acid Oxidoreductases / Q000737:chemistry*; D002352:Carrier Proteins / Q000737:chemistry*; D007887:Fabaceae / Q000201:enzymology*; D050959:Glycine Decarboxylase Complex; D050961:Glycine Decarboxylase Complex H-Protein; D050841:Glycine Dehydrogenase (Decarboxylating); D008928:Mitochondria / Q000201:enzymology; D010946:Plants, Medicinal; D011487:Protein Conformation; D014961:X-Ray Diffraction
D002352:Carrier Proteins; D050961:Glycine Decarboxylase Complex H-Protein; D000594:Amino Acid Oxidoreductases; D050959:Glycine Decarboxylase Complex; D050841:Glycine Dehydrogenase (Decarboxylating)