Crystallization and preliminary crystallographic analysis of the soluble alpha-glycerophosphate oxidase from Streptococcus sp.
Single crystals of soluble FAD-dependent alpha-glycerophosphate oxidase (GlpO) from Streptococcus sp. were obtained using the microseeding and hanging-drop vapor-equilibrium methods. Synchrotron X-ray radiation was used to collect diffraction data to 2.4 A resolution from these crystals. GlpO shares >30% identity with several bacterial and mitochondrial alpha-glycerophosphate dehydrogenases, although the GlpOs contain a 50-52-residue unique insert that appears to be important for efficient flavin reduction. The present work is an important first step in determining the structure of GlpO, which should provide insights on the function of this interesting flavoenzyme and its homologs.
Finnerty
Casey M
CM
Department of Molecular Biology and Genetics, Cornell University, Ithaca, NY 14853, USA.
Charrier
Véronique
V
Claiborne
Al
A
Karplus
P Andrew
PA
D003460:Crystallization; D018360:Crystallography, X-Ray; D005993:Glycerolphosphate Dehydrogenase / Q000737:chemistry*; D011487:Protein Conformation; D012995:Solubility; D013291:Streptococcus / Q000201:enzymology*
D005993:Glycerolphosphate Dehydrogenase