TRANSFERRED NUCLEAR OVERHAUSER EFFECT STUDY OF THE C-TERMINAL HELIX OF YEAST PHOSPHOGLYCERATE KINASE - NMR SOLUTION STRUCTURE OF THE C-TERMINAL BOUND PEPTIDE

Two-dimensional H-1 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-protei n complex are followed by transferred nuclear Overhauser effect spectr oscopy. Measurement of transferred NOEs and molecular modeling reveal an alpha-helix fold in the 405-409 region. This fold is in good agreem ent with the corresponding helix XIV of the crystallographic structure of wild-type PGK (Watson et al., 1982). The role of the alpha-helix f rom the C-terminal peptide in the recovery of catalytic activity in th e mutant PGK is discussed.