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Plant DHDPR forms a dimer with unique secondary structure features that preclude higher-order assembly.

Serena A J Watkin1, Jeremy R Keown1,2, Eric Richards1

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Summary

Plant dihydrodipicolinate reductase (DHDPR) enzymes are dimeric, unlike bacterial tetrameric forms. Unique structural features and substrate inhibition in plant DHDPR impact lysine biosynthesis.

Keywords:
enzyme kineticslysine biosynthesisoligomerisationprotein evolution

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Area of Science:

  • Biochemistry
  • Structural Biology
  • Plant Science

Background:

  • Dihydrodipicolinate reductase (DHDPR) is crucial for lysine biosynthesis in bacteria and plants.
  • Bacterial DHDPR enzymes are typically tetrameric, while plant DHDPR structures were previously unknown.

Purpose of the Study:

  • To determine the structures of plant DHDPR enzymes.
  • To compare the structural and functional differences between plant and bacterial DHDPR.
  • To investigate the implications for lysine biosynthesis in plants.

Main Methods:

  • X-ray crystallography was used to determine the structures of DHDPR from *Arabidopsis thaliana*, *Selaginella moellendorffii*, and *Neisseria meningitidis*.
  • Enzyme activity assays were performed to measure substrate inhibition.
  • Bioinformatic analysis of structural features was conducted.

Main Results:

  • Plant DHDPR from *V. vinifera*, *S. moellendorffii*, and *A. thaliana* are dimeric, contrasting with tetrameric bacterial enzymes.
  • The first crystal structures of dimeric plant DHDPR reveal unique secondary features preventing tetramer formation.
  • Plant DHDPR exhibits greater substrate inhibition due to increased flexibility and higher nucleotide affinity.
  • The structure of tetrameric bacterial DHDPR from *N. meningitidis* was also determined.

Conclusions:

  • Plant DHDPR enzymes possess a distinct dimeric structure that inhibits tetramer assembly.
  • Increased substrate inhibition in plant DHDPR, driven by structural flexibility, may affect strategies for enhancing plant lysine production.