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Structure and activity of particulate methane monooxygenase arrays in methanotrophs

Author

Listed:
  • Yanan Zhu

    (University of Oxford)

  • Christopher W. Koo

    (Northwestern University)

  • C. Keith Cassidy

    (University of Oxford)

  • Matthew C. Spink

    (Diamond Light Source, Harwell Science and Innovation Campus)

  • Tao Ni

    (University of Oxford)

  • Laura C. Zanetti-Domingues

    (Rutherford Appleton Laboratory)

  • Benji Bateman

    (Rutherford Appleton Laboratory)

  • Marisa L. Martin-Fernandez

    (Rutherford Appleton Laboratory)

  • Juan Shen

    (University of Oxford)

  • Yuewen Sheng

    (Diamond Light Source, Harwell Science and Innovation Campus)

  • Yun Song

    (Diamond Light Source, Harwell Science and Innovation Campus)

  • Zhengyi Yang

    (Diamond Light Source, Harwell Science and Innovation Campus
    European Molecular Biology Laboratory)

  • Amy C. Rosenzweig

    (Northwestern University)

  • Peijun Zhang

    (University of Oxford
    Diamond Light Source, Harwell Science and Innovation Campus
    University of Oxford)

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.

Suggested Citation

  • Yanan Zhu & Christopher W. Koo & C. Keith Cassidy & Matthew C. Spink & Tao Ni & Laura C. Zanetti-Domingues & Benji Bateman & Marisa L. Martin-Fernandez & Juan Shen & Yuewen Sheng & Yun Song & Zhengyi , 2022. "Structure and activity of particulate methane monooxygenase arrays in methanotrophs," Nature Communications, Nature, vol. 13(1), pages 1-10, December.
    • Handle: RePEc:nat:natcom:v:13:y:2022:i:1:d:10.1038_s41467-022-32752-9
    DOI: 10.1038/s41467-022-32752-9
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    References listed on IDEAS

    as
    1. Raquel L. Lieberman & Amy C. Rosenzweig, 2005. "Crystal structure of a membrane-bound metalloenzyme that catalyses the biological oxidation of methane," Nature, Nature, vol. 434(7030), pages 177-182, March.
    2. Ricardo M. Sanchez & Yingyi Zhang & Wenbo Chen & Lea Dietrich & Mikhail Kudryashev, 2020. "Subnanometer-resolution structure determination in situ by hybrid subtomogram averaging - single particle cryo-EM," Nature Communications, Nature, vol. 11(1), pages 1-7, December.
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