title: Expression, purification, crystallization and preliminary X-ray analysis of an NADP-dependent glyceraldehyde-3-phosphate dehydrogenase from Helicobacter pylori.
abstract: The classical glycolytic pathway contains an NAD-dependent glyceraldehyde-3-phosphate dehydrogenase, with NADP-dependent forms reserved for photosynthetic organisms and archaea. Here, the cloning, expression, purification, crystallization and preliminary X-ray analysis of an NADP-dependent glyceraldehyde-3-phosphate dehydrogenase from Helicobacter pylori is reported; crystals of the protein were grown both in the presence and the absence of NADP.
authors.affiliation: Henry Wellcome Laboratories for Structural Biology, Department of Biochemistry, University of Leicester, Leicester LE1 9HN, England.
authors.forename: Paul R
authors.initials: PR
authors.lastname: Elliott
authors.forename: Daniel
authors.initials: D
authors.lastname: Evans
authors.forename: Jacqueline A
authors.initials: JA
authors.lastname: Greenwood
authors.forename: Peter C E
authors.initials: PC
authors.lastname: Moody
mesh_terms: D001483:Base Sequence; D001665:Binding Sites; D003001:Cloning, Molecular; D003460:Crystallization; D018360:Crystallography, X-Ray; D017931:DNA Primers; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism; D016480:Helicobacter pylori / Q000201:enzymology*; D009249:NADP / Q000378:metabolism*; D011487:Protein Conformation
chemical_list: D017931:DNA Primers; D009249:NADP; D005987:Glyceraldehyde-3-Phosphate Dehydrogenases