Recovery of particulate methane monooxygenase structure and activity in a lipid bilayer

Koo, Christopher W.; Tucci, Frank J.; He, Yuan; Rosenzweig, Amy C.

doi:10.1126/science.abm3282

Recovery of particulate methane monooxygenase structure and activity in a lipid bilayer

Journal Article · 18 March 2022 · Science

DOI:https://doi.org/10.1126/science.abm3282· OSTI ID:1982957

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Department of Molecular Biosciences, Northwestern University, Evanston, IL 60208, USA.
Department of Molecular Biosciences, Northwestern University, Evanston, IL 60208, USA.; Department of Chemistry, Northwestern University, Evanston, IL 60208, USA.

Bacterial methane oxidation using the enzyme particulate methane monooxygenase (pMMO) contributes to the removal of environmental methane, a potent greenhouse gas. Crystal structures determined using inactive, detergent-solubilized pMMO lack several conserved regions neighboring the proposed active site. We show that reconstituting pMMO in nanodiscs with lipids extracted from the native organism restores methane oxidation activity. Multiple nanodisc-embedded pMMO structures determined by cryo–electron microscopy to 2.14- to 2.46-angstrom resolution reveal the structure of pMMO in a lipid environment. The resulting model includes stabilizing lipids, regions of the PmoA and PmoC subunits not observed in prior structures, and a previously undetected copper-binding site in the PmoC subunit with an adjacent hydrophobic cavity. These structures provide a revised framework for understanding and engineering pMMO function.

Research Organization:: Pacific Northwest National Laboratory (PNNL), Richland, WA (United States). Environmental Molecular Sciences Laboratory (EMSL)

Sponsoring Organization:: USDOE

DOE Contract Number:: AC05-76RL01830

OSTI ID:: 1982957

Journal Information:: Science, Vol. 375, Issue 6586; ISSN 0036-8075

Publisher:: AAAS

Country of Publication:: United States

Language:: English

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