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Related Experiment Videos

Induced fit on sugar binding activates ribokinase.

J A Sigrell1, A D Cameron, S L Mowbray

  • 1Department of Molecular Biology, Uppsala University, Uppsala, Sweden.

Journal of Molecular Biology
|August 10, 1999
PubMed
Summary
This summary is machine-generated.

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Ribokinase uses large and small conformational changes to bind ribose and ATP, facilitating sugar metabolism. These structural shifts are crucial for enzyme function and catalysis.

Area of Science:

  • Biochemistry
  • Structural Biology
  • Enzymology

Background:

  • Ribokinase catalyzes the initial phosphorylation of ribose, a key step in its metabolic pathway.
  • Previous structural data existed for the ternary complex of Escherichia coli ribokinase with ribose and ADP.

Purpose of the Study:

  • To elucidate the conformational changes involved in ribokinase function through structural analysis.
  • To understand the mechanism of substrate binding and catalysis in ribokinase.

Main Methods:

  • X-ray crystallography was employed to determine structures of the apo enzyme, ribose-bound state, and four new ternary complex forms.
  • Comparative structural analysis was performed to identify conformational differences.

Main Results:

Related Experiment Videos

  • Structures reveal an open apo form that transitions to a closed conformation upon ribose binding, trapping the sugar.
  • Nucleotide binding induces further, subtle structural adjustments in the enzyme.
  • Evidence suggests lid movements in the ternary complex are essential for transition state formation and breakdown.

Conclusions:

  • Conformational changes, both large and small, are critical for ribokinase activity.
  • The observed structural dynamics provide insights into the catalytic mechanism of ribokinase and related carbohydrate kinases.
  • These findings have implications for understanding enzyme function in sugar metabolism.