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- Title
Structure and activity of particulate methane monooxygenase arrays in methanotrophs.
- Authors
Zhu, Yanan; Koo, Christopher W.; Cassidy, C. Keith; Spink, Matthew C.; Ni, Tao; Zanetti-Domingues, Laura C.; Bateman, Benji; Martin-Fernandez, Marisa L.; Shen, Juan; Sheng, Yuewen; Song, Yun; Yang, Zhengyi; Rosenzweig, Amy C.; Zhang, Peijun
- 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. Particulate methane monooxygenase (pMMO) is the main enzyme used by methanotrophs. Here, the authors determined the native structure of pMMO by cryo-electron tomography, revealing lipid-stabilized features and a higher-order hexagonal array arrangement in intact cells.
- Subjects
MONOOXYGENASES; GREENHOUSE gas mitigation; METHANOTROPHS; METHANE; SCANNING electron microscopes
- Publication
Nature Communications, 2022, Vol 13, Issue 1, p1
- ISSN
2041-1723
- Publication type
Article
- DOI
10.1038/s41467-022-32752-9