EMD-14530
pMMO three trimer interaction map from native membrane
EMD-14530
Subtomogram averaging12.0 Å
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Map released: 10/08/2022
Last modified: 22/02/2023
Sample Organism:
Methylococcus capsulatus str. Bath
Sample: pMMO
Deposition Authors: Zhu Y
,
Ni T
,
Zhang P
Sample: pMMO
Deposition Authors: Zhu Y
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Structure and activity of particulate methane monooxygenase arrays in methanotrophs.
Zhu Y
,
Koo CW,
Cassidy CK
,
Spink MC,
Ni T
,
Zanetti-Domingues LC
,
Bateman B
,
Martin-Fernandez ML
,
Shen J,
Sheng Y
,
Song Y
,
Yang Z
,
Rosenzweig AC
,
Zhang P
(2022) Nat Commun , 13 , 5221 - 5221
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(2022) Nat Commun , 13 , 5221 - 5221
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.
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.