7S4I

CryoEM structure of Methylococcus capsulatus (Bath) pMMO in a native lipid nanodisc at 2.26 Angstrom resolution

Summary for 7S4I

• Entry DOI: 10.2210/pdb7s4i/pdb
• EMDB information: 24826 24827 24828 24829 24830 24831
• Descriptor: Particulate methane monooxygenase alpha subunit, Ammonia monooxygenase/methane monooxygenase, subunit C family protein, Particulate methane monooxygenase beta subunit, ... (9 entities in total)
• Functional Keywords: complex, oxidoreductase
• Biological source: Methylococcus capsulatus str. Bath; More
• Total number of polymer chains: 9
• Total formula weight: 337114.29

Authors

Koo, C.W.,Rosenzweig, A.C. (deposition date: 2021-09-09, release date: 2022-03-30, Last modification date: 2024-06-05)

Primary citation

Koo, C.W.,Tucci, F.J.,He, Y.,Rosenzweig, A.C.
Recovery of particulate methane monooxygenase structure and activity in a lipid bilayer.
Science, 375:1287-1291, 2022

PubMed Abstract: 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.

PubMed: 35298269
DOI: 10.1126/science.abm3282

Experimental method

ELECTRON MICROSCOPY (2.26 Å)