6b9s | pdb_00006b9s
From Proteopedia
MPnS crystallized in the absence of substrate
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Structural highlights
Function[MPNS_NITMS] Catalyzes the conversion of 2-hydroxyethylphosphonate into methylphosphonate in the methylphosphonate biosynthesis pathway.[1] Publication Abstract from PubMedMethylphosphonate 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
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This page was last modified 09:50, 4 December 2019.