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Article: Structure and activity of particulate methane monooxygenase arrays in methanotrophs

TitleStructure and activity of particulate methane monooxygenase arrays in methanotrophs
Authors
Issue Date5-Sep-2022
PublisherNature Research
Citation
Nature Communications, 2022, v. 13, n. 1 How to Cite?
AbstractMethane-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.
Persistent Identifierhttp://hdl.handle.net/10722/340319
ISSN
2023 Impact Factor: 14.7
2023 SCImago Journal Rankings: 4.887
ISI Accession Number ID

 

DC FieldValueLanguage
dc.contributor.authorZhu, Y-
dc.contributor.authorKoo, CW-
dc.contributor.authorCassidy, CK-
dc.contributor.authorSpink, MC-
dc.contributor.authorNi, T-
dc.contributor.authorZanetti-Domingues, LC-
dc.contributor.authorBateman, B-
dc.contributor.authorMartin-Fernandez, ML-
dc.contributor.authorShen, J-
dc.contributor.authorSheng, Y-
dc.contributor.authorSong, Y-
dc.contributor.authorYang, Z-
dc.contributor.authorRosenzweig, AC-
dc.contributor.authorZhang, P-
dc.date.accessioned2024-03-11T10:43:15Z-
dc.date.available2024-03-11T10:43:15Z-
dc.date.issued2022-09-05-
dc.identifier.citationNature Communications, 2022, v. 13, n. 1-
dc.identifier.issn2041-1723-
dc.identifier.urihttp://hdl.handle.net/10722/340319-
dc.description.abstractMethane-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.-
dc.languageeng-
dc.publisherNature Research-
dc.relation.ispartofNature Communications-
dc.rightsThis work is licensed under a Creative Commons Attribution-NonCommercial-NoDerivatives 4.0 International License.-
dc.titleStructure and activity of particulate methane monooxygenase arrays in methanotrophs-
dc.typeArticle-
dc.identifier.doi10.1038/s41467-022-32752-9-
dc.identifier.scopuseid_2-s2.0-85137198839-
dc.identifier.volume13-
dc.identifier.issue1-
dc.identifier.eissn2041-1723-
dc.identifier.isiWOS:000850348400013-
dc.identifier.issnl2041-1723-

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