The magnesium protein interaction in nucleotide complexes of phos-phoglycerate kinase
The X-ray structure determination of yeast phosphoglycerate kinase and subsequent substrate binding studies have helped to define the binding sites for the triose and nucleoside phosphate substrates. This communication deals with one feature of the binding site—the location of an aspartic acid residue close to the phosphoryl binding site of the nucleotide substrate—and relates this and other structural features of the active site to the properties of this enzyme as deduced from nuclear magnetic resonance studies.
KeywordsEnzyme mechanism crystallography resonance phosphoryl
Unable to display preview. Download preview PDF.
- Blake, C. C. F. and Rice, D. W. (1981)Phil. Trans. R. Soc. London,B293, 93.Google Scholar
- Mildvan, A. S. (1981)Phil. Trans. R. Soc. London,B293, 65.Google Scholar
- Watson, H. C., Walker, N. P. C., Shaw, P. J., Bryant, T. N., Wendell, P. L., Fothergill, L. A., Perkins, R. E., Conroy, S. C., Dobson, M. J., Tuite, M. F., Kingsman, A. J. and Kingsman, S. M. (1982)EMBOJ.,1, 1635.Google Scholar