7s4h

CryoEM structure of Methylococcus capsulatus (Bath) pMMO in a native lipid nanodisc at 2.14 Angstrom resolution

spinqualitylabelsall models 7s4h, resolution 2.14Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7s4h is a 9 chain structure with sequence from Methylococcus capsulatus str. Bath. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 2.14Å Ligands: CU, D10, HXG, P1O, PLC Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function PMOB_METCA Publication Abstract from PubMed 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. Recovery of particulate methane monooxygenase structure and activity in a lipid bilayer.,Koo CW, Tucci FJ, He Y, Rosenzweig AC Science. 2022 Mar 18;375(6586):1287-1291. doi: 10.1126/science.abm3282. Epub 2022 , Mar 17. PMID:35298269 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Methane monooxygenase 3D structures

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