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Structure of human phagocyte NADPH oxidase in the resting state
Open accessPreprint — published as 10.7554/elife.83743 · Paper page
Abstract
Phagocyte oxidase plays an essential role in the first line of host defense against pathogens. It oxidizes intracellular NADPH to reduce extracellular oxygen to produce superoxide anions for pathogen killing. The resting phagocyte oxidase is a heterodimeric complex formed by two transmembrane proteins NOX2 and p22. Despite the functional importance of this complex, its structure remains elusive. Here we reported the cryo-EM structure of the human NOX2-p22 complex in nanodisc in the resting state. The structure shows that p22 is formed by four transmembrane helices and interacts with NOX2 through its M1 and M4 helices. Hydrophobic residues on M3, M4, and M5 of NOX2 contribute to the complex formation. Structural analysis suggests that the cytosolic factors activate the NOX2-p22 complex by stabilizing the dehydrogenase domain (DH) in a productive docked conformation which is efficient for electron transfer between DH and the transmembrane domain.
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Highly accurate protein structure prediction with AlphaFold
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Metadata
- Authors
- Liu, R., Song, K., Wu, J.-X., Geng, X.-P., Zheng, L., Gao, X., Peng, H., & Chen, L.
- Affiliations
- Peking University (CN)
- Corresponding author
- Chen, Lei
- Venue
- eLife
- Publisher
- openRxiv
- Published
- 2022-10-04
- Volume
- 11
- ISSN
- 2050-084X (ISSN-L)
- PMC
- PMC9711523
- OpenAlex
- W4309575422
- Cited by
- 63
- References
- 1
- Citations by year
- 2026: 13 · 2025: 14 · 2024: 20 · 2023: 15
- FWCI
- 4.68
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Licence
- cc-by
- Locations
- eLife (publishedVersion, cc-by)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Greater South Information System
- Funders
- National Natural Science Foundation of China (91957201, 31870833 and 31821091, 52021 006, 2020-01, 31870833, 91957201, 31821091)
- Peking University
- Center for Life Sciences
- National Key Research and Development Program of China (31821091, 202001, 2022YFA1303000)
- Beijing National Laboratory for Molecular Sciences (BNLMS- CXTD-202001, CXTD‐202001)
- Topics
- Life Sciences › Immunology and Microbiology › Immunology › Neutrophil, Myeloperoxidase and Oxidative Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
- Keywords
- NADPH oxidase, NOX2, p22phox, heterodimer, nanodiscs, transmembrane helices, electron transfer, NADPH binding, superoxide, host defense
- MeSH terms
- Humans, Membrane Proteins, NADP, Phagocytes, Superoxides, NADPH Oxidases
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