EMD-14530

Subtomogram averaging
12.0 Å
EMD-14530 Deposition: 14/03/2022
Map released: 10/08/2022
Last modified: 22/02/2023
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links

EMD-14530

pMMO three trimer interaction map from native membrane

EMD-14530

Subtomogram averaging
12.0 Å
EMD-14530 Deposition: 14/03/2022
Map released: 10/08/2022
Last modified: 22/02/2023
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Sample Organism: Methylococcus capsulatus str. Bath
Sample: pMMO

Deposition Authors: Zhu Y , Ni T , Zhang P
Structure and activity of particulate methane monooxygenase arrays in methanotrophs.
PUBMED: 36064719
DOI: doi:10.1038/s41467-022-32752-9
ISSN: 2041-1723
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.