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 (Mr approximately 45,000) 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.
Fairbrother
W J
WJ
Inorganic Chemistry Laboratory, University of Oxford, England.
Bowen
D
D
Hall
L
L
Williams
R J
RJ
D000255:Adenosine Triphosphate / Q000378:metabolism; D005988:Glyceric Acids / Q000378:metabolism; D009682:Magnetic Resonance Spectroscopy; D010735:Phosphoglycerate Kinase; D015003:Yeasts / Q000201:enzymology*
D005988:Glyceric Acids; C005156:3-phosphoglycerate; D000255:Adenosine Triphosphate; D010735:Phosphoglycerate Kinase