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Structures of Mycobacterium tuberculosis isoprenyl diphosphate synthase Rv2173 in substrate-bound forms.

James A Titterington1, Ngoc Anh Thu Ho1, Charles P H Beasley2

  • 1Biomolecular Interaction Centre and School of Physical and Chemical Sciences, University of Canterbury. Christchurch, New Zealand.

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Summary

Structures of Mycobacterium tuberculosis isoprenyl diphosphate synthase Rv2173 reveal how substrate binding influences protein conformation. The C-terminus plays a key role in substrate entry and product release, suggesting a C10-C15 final product size.

Keywords:
Mycobacterium tuberculosisRv2173dimethylallyl diphosphateisoprenyl diphosphateisoprenyl diphosphate synthases

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Enzymology

Background:

  • Isoprenyl diphosphate synthases are crucial enzymes in the biosynthesis of isoprenoids.
  • Mycobacterium tuberculosis Rv2173 is a trans-isoprenyl diphosphate synthase with uncertain product length.
  • Understanding Rv2173 structure-function relationships is important for targeting essential metabolic pathways.

Purpose of the Study:

  • To elucidate the structural basis of Rv2173 activity.
  • To investigate the role of substrate binding and metal ions in enzyme conformation.
  • To determine the likely product length of Rv2173.

Main Methods:

  • X-ray crystallography was used to determine the structures of Rv2173 in apo, IPP-bound, and DMAPP-bound states.
  • Structural comparisons were made between the different forms and with other isoprenyl diphosphate synthases.

Main Results:

  • Rv2173 adopts a canonical all-alpha-helical trans-isoprenyl diphosphate synthase fold and exists as a dimer.
  • Substrate binding (IPP and DMAPP) induces conformational changes, particularly involving the C-terminus.
  • The C-terminus appears to regulate substrate entry and product exit.
  • The binding of IPP and DMAPP involves different numbers of metal ions and slightly different poses.
  • Structural features suggest Rv2173 produces C10-C15 isoprenoids.

Conclusions:

  • The structure of Rv2173 provides insights into the mechanism of trans-isoprenyl diphosphate synthases.
  • The C-terminal region is critical for Rv2173 function.
  • Rv2173 likely synthesizes C10-C15 isoprenoid products.