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6B9T

Crystal structure of MPnS with substrate 2-hydroxyethylphosphonate (2-HEP) and Fe(II) bound

Summary for 6B9T
Entry DOI10.2210/pdb6b9t/pdb
DescriptorMethylphosphonate synthase, FE (III) ION, (2-hydroxyethyl)phosphonic acid, ... (5 entities in total)
Functional Keywordsphosphonate, methylphosphonate, iron, oxidoreductase
Biological sourceNitrosopumilus maritimus (strain SCM1)
Total number of polymer chains8
Total formula weight418701.86
Authors
Born, D.A.,Drennan, C.L. (deposition date: 2017-10-11, release date: 2017-12-20, Last modification date: 2024-03-13)
Primary citationBorn, D.A.,Ulrich, E.C.,Ju, K.S.,Peck, S.C.,van der Donk, W.A.,Drennan, C.L.
Structural basis for methylphosphonate biosynthesis.
Science, 358:1336-1339, 2017
Cited by
PubMed 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 (HEPD), and find that it displays the same motif. HEPD 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 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.
PubMed: 29217579
DOI: 10.1126/science.aao3435
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.35 Å)
Structure validation

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