Journal
SCIENCE
Volume 375, Issue 6586, Pages 1287-+Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.abm3282
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Funding
- National Institutes of Health [R35GM118035, T32GM008382, T32GM105538, R01GM135651, U24GM129547]
- NCI CCSG [P30 CA060553]
- Office of Biological and Environmental Research [grid.436923.9]
- NIH Common Fund Transformative High-Resolution Cryoelectron Microscopy program [U24 GM129541, U24 GM129539]
- Simons Foundation [SF349247]
- NY State Assembly
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Bacterial methane oxidation using pMMO can be restored by reconstitution in nanodiscs, and the structures of pMMO in a lipid environment have been determined by cryo-electron microscopy. These findings provide important insights for understanding and engineering the function of pMMO.
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 nanodiscembedded 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.
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