• Corpus ID: 103741204

Cryocrystallographic and mechanistic studies on glycogen phosphorylase

  title={Cryocrystallographic and mechanistic studies on glycogen phosphorylase},
  author={Edward P Mitchell},
Glycogen phosphorylase (GPb) regulates the degradation of glycogen to glucose-1-phosphate and catalyses the first step of the reaction. Many studies have provided insights into the essentials of the catalytic mechanism. Previous time resolved crystallographic work using heptenitol has revealed a putative phosphate binding site at the active site of phosphorylase. Using nojirimycin tetrazole, a transition state analogue, complexed with phosphate and both T and R state GPb crystals, this work has… 
Effects of commonly used cryoprotectants on glycogen phosphorylase activity and structure
Experimental investigation by X‐ray crystallography showed that both MPD and DMSO do not bind at the catalytic site, do not induce any significant conformational change on the enzyme molecule, and hence, are more suitable cryoprotectants than glycerol for binding studies with glycogen phosphorylase.
The structure of a glycogen phosphorylase glucopyranose spirohydantoin complex at 1.8 Å resolution and 100 K: The role of the water structure and its contribution to binding
Analysis of the water structure at the catalytic site of the native enzyme, shows that five waters are displaced by ligand binding and that there is a significant decrease in mobility of the remaining waters on formation of the GPb‐hydantoin complex.


Glycogen Phosphorylase B: Description of the Protein Structure
It is shown that the large protein conforms to the rules deduced from smaller protein molecules and provides examples of almost every structural feature.
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Oscillation data reduction pro gram in 'Data Collection and Process­ ing' , ed
  • G. Sawyer, L. Isaacs and S. Bailey, pp 56 -62. SERC Daresbury Laboratory DL/
  • 1993
Acta Cryst
  • A42, 140-149.
  • 1986
Methods in Enzymology: Vol.93, Part F
DPhil Thesis, Oxford University, UK
  • Mitchell, E. P. & Carman, E. F. (1994). /. Appl. Cryst. 27, 1070-1074.
  • 1985
Acta Cryst
  • B44, 22-26.
  • 1988
  • Carb. Chem. Biochem. 48, 319-384. Leonidas, D. D., Oikonomakos, N. G., Papageorgiou, A. C. & Sotiroudis, T. G. (1992). Protein Science 1, 1123-1132.
  • 1990
Data Collection and Processing, edited
  • 1993
The Enzymes, 3rd edition, edited by P Boyer, pp 435-482
  • 1972