Sequence and structure of yeast phosphoglycerate kinase. |
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| Authors: | H C Watson N P Walker P J Shaw T N Bryant P L Wendell L A Fothergill R E Perkins S C Conroy M J Dobson M F Tuite et al. |
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| Affiliation: | H C Watson, N P Walker, P J Shaw, T N Bryant, P L Wendell, L A Fothergill, R E Perkins, S C Conroy, M J Dobson, M F Tuite, et al. |
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| Abstract: | 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. |
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