Ternary complex crystal structures of glycogen phosphorylase with the transition state analogue nojirimycin tetrazole and phosphate in the T and R states.

@article{Mitchell1996TernaryCC,
  title={Ternary complex crystal structures of glycogen phosphorylase with the transition state analogue nojirimycin tetrazole and phosphate in the T and R states.},
  author={Edward P Mitchell and Stephen G. Withers and Philipp Ermert and Andrea Vasella and Elspeth F. Garman and Nikos G. Oikonomakos and Louise N. Johnson},
  journal={Biochemistry},
  year={1996},
  volume={35 23},
  pages={
          7341-55
        }
}
Catalysis by glycogen phosphorylase involves a mechanism in which binding of one substrate tightens the binding of the other substrate to produce a productive ternary enzyme-substrate complex. In this work the molecular basis for this synergism is probed in crystallographic studies on ternary complexes in which the glucosyl component is substituted by the putative transition state analogue nojirimycin tetrazole, a compound which has been established previously as a transition state analogue… 
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