TY - JOUR
T1 - Structural basis for methylphosphonate biosynthesis
AU - Born, David A.
AU - Ulrich, Emily C.
AU - Ju, Kou San
AU - Peck, Spencer C.
AU - Van Der Donk, Wilfred A.
AU - Drennan, Catherine L.
N1 - Funding Information:
We thank the Giovannoni laboratory for genomic DNA from P. ubique HTCC7217 and H. Cooke for the plasmids for NmMPnS-Q152A and Q152E. This work was supported by the National Institutes of Health (GM 077596 to W.A.V.). An NIH Molecular Biophysics Training Grant T32 GM008313 supported D.A.B. C.L.D. and W.A.V. are Howard Hughes Medical Institute Investigators. 31P NMR data were collected on a 600-MHz NMR spectrometer funded by NIH (S10-RR028833). This work used Northeastern Collaborative Access Team beamlines (GM103403) and a Pilatus detector (RR029205) at the Advanced Photon Source (DE-AC02-06CH11357). Structures of 2-HEP-bound Fe(II)-SaHEPD, substrate-free MPnS, and 2-HEP-bound Fe(II)-MPnS are available through the Protein Data Bank under accession codes 6B9R, 6B9S, and 6B9T, respectively.
Publisher Copyright:
© 2017, American Association for the Advancement of Science. All rights reserved.
PY - 2017/12/8
Y1 - 2017/12/8
N2 - 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.
AB - 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.
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U2 - 10.1126/science.aao3435
DO - 10.1126/science.aao3435
M3 - Article
C2 - 29217579
AN - SCOPUS:85037667857
SN - 0036-8075
VL - 358
SP - 1336
EP - 1339
JO - Science
JF - Science
IS - 6368
ER -