Structural highlights
Function
[MPNS_NITMS] Catalyzes the conversion of 2-hydroxyethylphosphonate into methylphosphonate in the methylphosphonate biosynthesis pathway.[1]
Publication Abstract from PubMed
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.
Structural basis for methylphosphonate biosynthesis.,Born DA, Ulrich EC, Ju KS, Peck SC, van der Donk WA, Drennan CL Science. 2017 Dec 8;358(6368):1336-1339. doi: 10.1126/science.aao3435. PMID:29217579[2]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Metcalf WW, Griffin BM, Cicchillo RM, Gao J, Janga SC, Cooke HA, Circello BT, Evans BS, Martens-Habbena W, Stahl DA, van der Donk WA. Synthesis of methylphosphonic acid by marine microbes: a source for methane in the aerobic ocean. Science. 2012 Aug 31;337(6098):1104-7. doi: 10.1126/science.1219875. PMID:22936780 doi:http://dx.doi.org/10.1126/science.1219875
- ↑ Born DA, Ulrich EC, Ju KS, Peck SC, van der Donk WA, Drennan CL. Structural basis for methylphosphonate biosynthesis. Science. 2017 Dec 8;358(6368):1336-1339. doi: 10.1126/science.aao3435. PMID:29217579 doi:http://dx.doi.org/10.1126/science.aao3435