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Crystal structure of acetoacetyl-CoA reductase from Rickettsia felis

Justas V Rodarte1, Jan Abendroth2, Thomas E Edwards2

  • 1Department of Chemistry, Vassar College, 124 Raymond Avenue, Poughkeepsie, New York, USA.

Acta Crystallographica. Section F, Structural Biology Communications
|February 23, 2021
PubMed

Insights

The structure of Rickettsia felis acetoacetyl-CoA reductase was determined. This enzyme shares a common fold with other short-chain dehydrogenase/reductase (SDR) family members, offering potential therapeutic targets.

Area of Science:

  • Microbiology
  • Structural Biology
  • Biochemistry

Background:

  • Rickettsia felis is an emerging Gram-negative bacterial pathogen causing spotted fever and is a priority pathogen.
  • Increasing adaptability to diverse hosts leads to fevers of unknown origin being attributed to R. felis.
  • Understanding Rickettsia proteomes can reveal novel therapeutic strategies.

Purpose of the Study:

  • To determine the three-dimensional structure of acetoacetyl-CoA reductase from Rickettsia felis.
  • To compare the structure of R. felis acetoacetyl-CoA reductase with homologous enzymes.
  • To identify potential therapeutic targets through comparative structural analysis.

Main Methods:

  • X-ray crystallography was used to determine the structure of R. felis acetoacetyl-CoA reductase.
  • The structure was resolved to a resolution of 2.0 Å.
  • Sequence identity and structural fold comparisons were performed with known homologs.

Main Results:

  • The crystal structure of Rickettsia felis acetoacetyl-CoA reductase was elucidated at 2.0 Å resolution.
  • Despite less than 50% sequence identity to homologs, the enzyme adopts a conserved short-chain dehydrogenase/reductase (SDR) fold.
  • Structural similarities were observed with enzymes like FabG from Staphylococcus aureus and Bacillus anthracis.

Conclusions:

  • The determined structure provides insights into the R. felis acetoacetyl-CoA reductase.
  • The conserved SDR fold suggests potential functional roles and offers a basis for drug development.
  • Comparative proteomic and structural studies of Rickettsia species are crucial for discovering new treatments.
Keywords:
PhaBRickettsiaSSGCIDSeattle Structural Genomics Center for Infectious Diseaseacetoacetyl-CoA reductaseoxidoreductasestructural genomics

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