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Structural basis for methylphosphonate biosynthesis.

David A Born1,2, Emily C Ulrich3,4, Kou-San Ju4,5,6

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|December 9, 2017
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Methylphosphonate synthase (MPnS) produces methylphosphonate, a key methane precursor in the ocean. Researchers elucidated its structure and identified key residues for methylphosphonate synthesis, revealing its widespread presence in marine microbes.

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Area of Science:

  • Biochemistry
  • Environmental Microbiology
  • Structural Biology

Background:

  • Methylphosphonate is a crucial metabolic precursor to methane in marine environments.
  • Understanding the enzymes involved in methylphosphonate metabolism is vital for marine biogeochemical cycling.

Purpose of the Study:

  • To determine the high-resolution structure of methylphosphonate synthase (MPnS).
  • To identify the molecular determinants for methylphosphonate synthesis.
  • To investigate the prevalence of MPnS in marine ecosystems.

Main Methods:

  • X-ray crystallography was used to determine the 2.35-angstrom resolution structure of MPnS.
  • Structural analysis and site-directed mutagenesis were employed to understand enzyme function.
  • Bioinformatic analysis of marine microbiomes was conducted to identify putative MPnS sequences.

Main Results:

  • The structure of MPnS revealed an unusual 2-histidine-1-glutamine iron-coordinating triad.
  • Hydroxyethylphosphonate dioxygenase (HEPD) from *Streptomyces albus* shares this motif and can be converted to MPnS via mutation.
  • Putative MPnS enzymes were identified across diverse marine microbiomes, including in *Pelagibacter ubique*.

Conclusions:

  • The 2-histidine-1-glutamine motif is critical for methylphosphonate synthesis.
  • MPnS is widespread in marine environments, supporting the role of methylphosphonate as a methane source.
  • Marine microbes utilize methylphosphonate as a phosphorus source in phosphorus-limited conditions.