Publication Abstract from PubMed
Two crystalline forms of GADPH (D-glyceraldehyde-3-phosphate dehydrogenase) from Spinacia oleracea were obtained using sitting-drop vapor diffusion. Despite the very low concentration of GADPH in the solutions, two crystalline forms were obtained, one of which was the previously reported C222 space group with unit-cell parameters a = 155.3, b = 181.7, c = 107.6 A and the other of which belonged to a new space group I4(1)22, with unit-cell parameters a = b = 120.9, c = 154.5 A. Diffraction data were measured from both native and derivatives, yielding structures at a resolution limit of 3.0 A. Differences at the NAD(+)/NADP(+)-binding site seen in these structures compared with the previously reported structure with bound coenzyme suggest that conformational changes associated with pyridine-nucleotide binding may play a role in the regulation of this enzyme.
Crystallization and structural analysis of GADPH from Spinacia oleracea in a new form.,Camara-Artigas A, Hirasawa M, Knaff DB, Wang M, Allen JP Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Nov 1;62(Pt, 11):1087-92. Epub 2006 Oct 25. PMID:17077485[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
