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Science. 2017 Dec 8;358(6368):1336-1339. doi: 10.1126/science.aao3435.

Structural basis for methylphosphonate biosynthesis.

Author information

1
Graduate Program in Biophysics, Harvard University, Cambridge, MA, USA.
2
Department of Biology, Massachusetts Institute of Technology, Cambridge, MA, USA.
3
Department of Chemistry, University of Illinois at Urbana-Champaign, Urbana, IL, USA.
4
Carl R. Woese Institute for Genomic Biology, University of Illinois at Urbana-Champaign, Urbana, IL, USA.
5
Department of Microbiology, The Ohio State University, Columbus, OH, USA.
6
Division of Medicinal Chemistry and Pharmacognosy, The Ohio State University, Columbus, OH, USA.
7
Howard Hughes Medical Institute, University of Illinois at Urbana-Champaign, Urbana, IL, USA.
8
Department of Chemistry, Massachusetts Institute of Technology, Cambridge, MA, USA.
9
Howard Hughes Medical Institute, Massachusetts Institute of Technology, Cambridge, MA, USA.

Abstract

Methylphosphonate synthase (MPnS) produces methylphosphonate, a metabolic precursor to methane in the upper ocean. Here, we determine a 2.35-angstrom resolution structure of MPnS and discover that it has an unusual 2-histidine-1-glutamine iron-coordinating triad. We further solve the structure of a related enzyme, hydroxyethylphosphonate dioxygenase from Streptomyces albus (SaHEPD), and find that it displays the same motif. SaHEPD can be converted into an MPnS by mutation of glutamine-adjacent residues, identifying the molecular requirements for methylphosphonate synthesis. Using these sequence markers, we find numerous putative MPnSs in marine microbiomes and confirm that MPnS is present in the abundant Pelagibacter ubique. The ubiquity of MPnS-containing microbes supports the proposal that methylphosphonate is a source of methane in the upper, aerobic ocean, where phosphorus-starved microbes catabolize methylphosphonate for its phosphorus.

PMID:
29217579
PMCID:
PMC5901744
DOI:
10.1126/science.aao3435
[Indexed for MEDLINE]
Free PMC Article

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