One‐ and two‐dimensional NMR studies of yeast phosphoglycerate kinase

One‐ and two‐dimensional proton NMR studies have been carried out on yeast phosphoglycerate kinase ( M r ∼ 45000) in order to identify amino‐acid spin systems and obtain sequence‐specific assignments. A number of sequence‐specific assignments have been made using a combination of structural information contained in nuclear Overhauser effect spectra and X‐ray crystallographic data. The results of substrate binding studies (both 3‐phosphoglycerate and Mg · ATP), which indicate mutual reorientation of certain assigned aromatic residues in the inter‐domain region of the protein, are discussed.