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Related Experiment Videos

The integral membrane enzyme PagP alternates between two dynamically distinct states.

Peter M Hwang1, Russell E Bishop, Lewis E Kay

  • 1Department of Biochemistry, University of Toronto, Toronto, ON, Canada M5S 1A8.

Proceedings of the National Academy of Sciences of the United States of America
|June 24, 2004
PubMed
Summary

PhoPQ-activated gene P (PagP) enzyme dynamics were studied using NMR spectroscopy. PagP switches between flexible (R) and rigid (T) states, facilitating substrate entry and catalysis in Gram-negative bacteria.

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Enzymology

Background:

  • PhoPQ-activated gene P (PagP) is a Gram-negative bacterial enzyme.
  • PagP transfers palmitate from phospholipids to lipopolysaccharide.
  • X-ray crystallography revealed a central cavity for substrate binding in PagP.

Purpose of the Study:

  • Investigate the relationship between PagP enzyme dynamics and function.
  • Understand how PagP's structure facilitates its catalytic activity.

Main Methods:

  • Reconstituted PagP into CYFOS-7 detergent for activity.
  • Utilized (1)H-(15)N NMR spectroscopy to study enzyme kinetics and thermodynamics.
  • Analyzed chemical shift changes between different protein states.

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Main Results:

  • PagP exists in an equilibrium between relaxed (R) and tense (T) states.
  • The R to T transition has thermodynamic parameters: Delta H = -10.7 kcal/mol and Delta S = -37.5 cal/mol.K.
  • Significant structural changes occur in the L1 loop and beta barrel regions between R and T states.
  • The R state exhibits flexibility, aiding substrate entry, while the T state is rigid and catalytically important.

Conclusions:

  • PagP utilizes dynamic state switching for its catalytic cycle.
  • Protein flexibility in the R state facilitates substrate access.
  • The rigid T state adopts a conformation crucial for catalysis.