Publication Abstract from PubMed
The structure of yeast phosphoglycerate kinase has been determined with data obtained from amino acid sequence, nucleotide sequence, and X-ray crystallographic studies. The substrate binding sites, as deduced from electron density maps, are compatible with known substrate specificity and the stereochemical requirements for the enzymic reaction. A carboxyl-imidazole interaction appears to be involved in controlling the transition between the open and closed forms of the enzyme.
Sequence and structure of yeast phosphoglycerate kinase.,Watson HC, Walker NP, Shaw PJ, Bryant TN, Wendell PL, Fothergill LA, Perkins RE, Conroy SC, Dobson MJ, Tuite MF, et al. EMBO J. 1982;1(12):1635-40. PMID:6765200[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
