Structure and activity of particulate methane monooxygenase arrays in methanotrophs

DOI: 10.1038/s41467-022-32752-9

Authors: Yanan Zhu (Wellcome Trust Centre for Human Genetics, University of Oxford) , Christopher W. Koo (Northwestern University) , C. Keith Cassidy (University of Oxford) , Matthew C. Spink (Diamond Light Source) , Tao Ni (Wellcome Trust Centre for Human Genetics, University of Oxford) , Laura C. Zanetti-Domingues (Central Laser Facility, Science and Technology Facilities Council) , Benji Bateman (Central Laser Facility, Science and Technology Facility Council) , Marisa Martin-Fernandez (Central Laser Facility, Science and Technology Facilities Council) , Juan Shen (Wellcome Trust Centre for Human Genetics, University of Oxford) , Yuewen Sheng (Diamond Light Source) , Yun Song (Diamond Light Source) , Zhengyi Yang (Diamond Light Source) , Amy C. Rosenzweig (Northwestern University) , Peijun Zhang (Wellcome Trust Centre for Human Genetics, University of Oxford; Diamond Light Source; Chinese Academy of Medical Sciences Oxford Institute, University of Oxford)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Nature Communications , VOL 13

State: Published (Approved)
Published: September 2022
Diamond Proposal Number(s): 21004 , 29812

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.

Journal Keywords: Air microbiology; Cryoelectron microscopy; Cryoelectron tomography; Enzymes; Organelles

Diamond Keywords: Enzymes

Subject Areas: Biology and Bio-materials, Chemistry, Environment

Diamond Offline Facilities: Electron Bio-Imaging Centre (eBIC)
Instruments: Krios I-Titan Krios I at Diamond , Krios II-Titan Krios II at Diamond

Added On: 09/09/2022 10:43

Documents:
s41467-022-32752-9.pdf

Discipline Tags:

Earth Sciences & Environment Biotechnology Climate Change Biochemistry Chemistry Structural biology Engineering & Technology Life Sciences & Biotech

Technical Tags:

Imaging Tomography Cryo Electron Tomography (Cryo ET)