title: Transferred nuclear Overhauser effect study of the C-terminal helix of yeast phosphoglycerate kinase: NMR solution structure of the C-terminal bound peptide.
abstract: Two-dimensional 1H nuclear magnetic resonance spectroscopy is used to determine the structure of the C-terminal complementary peptide (404-415) bound to a mutant phosphoglycerate kinase (1-403). Conformational changes in the peptide induced by the formation of the peptide-protein complex are followed by transferred nuclear Overhauser effect spectroscopy. Measurement of transferred NOEs and molecular modeling reveal an alpha-helix fold in the 405-409 region. This fold is in good agreement with the corresponding helix XIV of the crystallographic structure of wild-type PGK (Watson et al., 1982). The role of the alpha-helix from the C-terminal peptide in the recovery of catalytic activity in the mutant PGK is discussed.
authors: Laboratoire de RMN, Centre National de la Recherche Scientifique, Gif sur Yvette, France.
authors: M
authors: M
authors: Andrieux
authors: E
authors: E
authors: Leroy
authors: E
authors: E
authors: Guittet
authors: M
authors: M
authors: Ritco-Vonsovici
authors: B
authors: B
authors: Mouratou
authors: P
authors: P
authors: Minard
authors: M
authors: M
authors: Desmadril
authors: J M
authors: JM
authors: Yon
mesh_terms: D018360:Crystallography, X-Ray; D006860:Hydrogen Bonding; D009682:Magnetic Resonance Spectroscopy; D010446:Peptide Fragments / Q000737:chemistry*; D010735:Phosphoglycerate Kinase / Q000737:chemistry* / Q000648:ultrastructure; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D012441:Saccharomyces cerevisiae / Q000201:enzymology; D012996:Solutions
chemical_list: D010446:Peptide Fragments; D012996:Solutions; D010735:Phosphoglycerate Kinase