title: Nuclear magnetic resonance studies of isolated structural domains of yeast phosphoglycerate kinase.
abstract: The structural integrity and substrate binding properties of the two genetically engineered domains of yeast phosphoglycerate kinase were investigated using one- and two-dimensional nuclear magnetic resonance techniques. Both domains were found to fold with regions of native-like structure, with the N-domain showing greater conformational flexibility than the C-domain. The 'basic patch' region of the N-domain is, however, clearly perturbed by removal of the C-domain. This is most likely due to the absence of stabilizing interactions between the C-terminal peptide (including alpha-helices XIII and XIV) and the N-domain. The C-domain is able to bind nucleotide with an affinity only three times less than that of the native protein.
authors.affiliation: Inorganic Chemistry Laboratory, University of Oxford, UK.
authors.forename: W J
authors.initials: WJ
authors.lastname: Fairbrother
authors.forename: P
authors.initials: P
authors.lastname: Minard
authors.forename: L
authors.initials: L
authors.lastname: Hall
authors.forename: J M
authors.initials: JM
authors.lastname: Betton
authors.forename: D
authors.initials: D
authors.lastname: Missiakas
authors.forename: J M
authors.initials: JM
authors.lastname: Yon
authors.forename: R J
authors.initials: RJ
authors.lastname: Williams
mesh_terms: D006863:Hydrogen-Ion Concentration; D009682:Magnetic Resonance Spectroscopy / Q000379:methods*; D009154:Mutation; D010735:Phosphoglycerate Kinase / Q000235:genetics; D011487:Protein Conformation; D012441:Saccharomyces cerevisiae / Q000201:enzymology* / Q000235:genetics; D013379:Substrate Specificity
chemical_list: D010735:Phosphoglycerate Kinase