7YZY

pMMO structure from native membranes by cryoET and STA

Summary for 7YZY

• Entry DOI: 10.2210/pdb7yzy/pdb
• EMDB information: 14399
• Descriptor: Particulate methane monooxygenase beta subunit, Methane monooxygenase subunit C2, Particulate methane monooxygenase alpha subunit (3 entities in total)
• Functional Keywords: pmmo, array, native membranes, membrane protein
• Biological source: Methylococcus capsulatus str. Bath; More
• Total number of polymer chains: 9
• Total formula weight: 323367.07

Authors

Zhu, Y.,Ni, T.,Zhang, P. (deposition date: 2022-02-21, release date: 2022-08-10, Last modification date: 2024-07-17)

Primary citation

Zhu, Y.,Koo, C.W.,Cassidy, C.K.,Spink, M.C.,Ni, T.,Zanetti-Domingues, L.C.,Bateman, B.,Martin-Fernandez, M.L.,Shen, J.,Sheng, Y.,Song, Y.,Yang, Z.,Rosenzweig, A.C.,Zhang, P.
Structure and activity of particulate methane monooxygenase arrays in methanotrophs.
Nat Commun, 13:5221-5221, 2022

PubMed Abstract: Methane-oxidizing bacteria play a central role in greenhouse gas mitigation and have potential applications in biomanufacturing. Their primary metabolic enzyme, particulate methane monooxygenase (pMMO), is housed in copper-induced intracytoplasmic membranes (ICMs), of which the function and biogenesis are not known. We show by serial cryo-focused ion beam (cryoFIB) milling/scanning electron microscope (SEM) volume imaging and lamellae-based cellular cryo-electron tomography (cryoET) that these ICMs are derived from the inner cell membrane. The pMMO trimer, resolved by cryoET and subtomogram averaging to 4.8 Å in the ICM, forms higher-order hexagonal arrays in intact cells. Array formation correlates with increased enzymatic activity, highlighting the importance of studying the enzyme in its native environment. These findings also demonstrate the power of cryoET to structurally characterize native membrane enzymes in the cellular context.

PubMed: 36064719
DOI: 10.1038/s41467-022-32752-9

Experimental method

ELECTRON MICROSCOPY (4.8 Å)