Skip to main content
bioRxiv
  • Home
  • About
  • Submit
  • ALERTS / RSS
Advanced Search
New Results

Structure of human phagocyte NADPH oxidase in the resting state

Rui Liu, View ORCID ProfileKangcheng Song, View ORCID ProfileJing-Xiang Wu, Xiao-Peng Geng, Liming Zheng, Xiaoyin Gao, Hailin Peng, View ORCID ProfileLei Chen
doi: https://doi.org/10.1101/2022.10.04.510768
Rui Liu
1State Key Laboratory of Membrane Biology, College of Future Technology, Institute of Molecular Medicine, Peking University, Beijing Key Laboratory of Cardiometabolic Molecular Medicine, Beijing 100871, China
2National Biomedical Imaging Center, Peking University, Beijing 100871, China
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
Kangcheng Song
1State Key Laboratory of Membrane Biology, College of Future Technology, Institute of Molecular Medicine, Peking University, Beijing Key Laboratory of Cardiometabolic Molecular Medicine, Beijing 100871, China
2National Biomedical Imaging Center, Peking University, Beijing 100871, China
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
  • ORCID record for Kangcheng Song
Jing-Xiang Wu
1State Key Laboratory of Membrane Biology, College of Future Technology, Institute of Molecular Medicine, Peking University, Beijing Key Laboratory of Cardiometabolic Molecular Medicine, Beijing 100871, China
2National Biomedical Imaging Center, Peking University, Beijing 100871, China
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
  • ORCID record for Jing-Xiang Wu
Xiao-Peng Geng
1State Key Laboratory of Membrane Biology, College of Future Technology, Institute of Molecular Medicine, Peking University, Beijing Key Laboratory of Cardiometabolic Molecular Medicine, Beijing 100871, China
2National Biomedical Imaging Center, Peking University, Beijing 100871, China
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
Liming Zheng
3Center for Nanochemistry, Beijing Science and Engineering Center for Nanocarbons, Beijing National Laboratory for Molecular Sciences, College of Chemistry and Molecular Engineering, Peking University, Beijing 100871, China
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
Xiaoyin Gao
3Center for Nanochemistry, Beijing Science and Engineering Center for Nanocarbons, Beijing National Laboratory for Molecular Sciences, College of Chemistry and Molecular Engineering, Peking University, Beijing 100871, China
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
Hailin Peng
3Center for Nanochemistry, Beijing Science and Engineering Center for Nanocarbons, Beijing National Laboratory for Molecular Sciences, College of Chemistry and Molecular Engineering, Peking University, Beijing 100871, China
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
Lei Chen
1State Key Laboratory of Membrane Biology, College of Future Technology, Institute of Molecular Medicine, Peking University, Beijing Key Laboratory of Cardiometabolic Molecular Medicine, Beijing 100871, China
2National Biomedical Imaging Center, Peking University, Beijing 100871, China
4Peking-Tsinghua Center for Life Sciences, Peking University, Beijing 100871, China
  • Find this author on Google Scholar
  • Find this author on PubMed
  • Search for this author on this site
  • ORCID record for Lei Chen
  • For correspondence: chenlei2016@pku.edu.cn
  • Abstract
  • Full Text
  • Info/History
  • Metrics
  • Preview PDF
Loading

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.

Competing Interest Statement

The authors have declared no competing interest.

Copyright 
The copyright holder for this preprint is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under a CC-BY 4.0 International license.
Back to top
PreviousNext
Posted October 04, 2022.
Download PDF
Email

Thank you for your interest in spreading the word about bioRxiv.

NOTE: Your email address is requested solely to identify you as the sender of this article.

Enter multiple addresses on separate lines or separate them with commas.
Structure of human phagocyte NADPH oxidase in the resting state
(Your Name) has forwarded a page to you from bioRxiv
(Your Name) thought you would like to see this page from the bioRxiv website.
CAPTCHA
This question is for testing whether or not you are a human visitor and to prevent automated spam submissions.
Share
Structure of human phagocyte NADPH oxidase in the resting state
Rui Liu, Kangcheng Song, Jing-Xiang Wu, Xiao-Peng Geng, Liming Zheng, Xiaoyin Gao, Hailin Peng, Lei Chen
bioRxiv 2022.10.04.510768; doi: https://doi.org/10.1101/2022.10.04.510768
Digg logo Reddit logo Twitter logo Facebook logo Google logo LinkedIn logo Mendeley logo
Citation Tools
Structure of human phagocyte NADPH oxidase in the resting state
Rui Liu, Kangcheng Song, Jing-Xiang Wu, Xiao-Peng Geng, Liming Zheng, Xiaoyin Gao, Hailin Peng, Lei Chen
bioRxiv 2022.10.04.510768; doi: https://doi.org/10.1101/2022.10.04.510768

Citation Manager Formats

  • BibTeX
  • Bookends
  • EasyBib
  • EndNote (tagged)
  • EndNote 8 (xml)
  • Medlars
  • Mendeley
  • Papers
  • RefWorks Tagged
  • Ref Manager
  • RIS
  • Zotero
  • Tweet Widget
  • Facebook Like
  • Google Plus One

Subject Area

  • Biochemistry
Subject Areas
All Articles
  • Animal Behavior and Cognition (4095)
  • Biochemistry (8791)
  • Bioengineering (6495)
  • Bioinformatics (23405)
  • Biophysics (11769)
  • Cancer Biology (9173)
  • Cell Biology (13302)
  • Clinical Trials (138)
  • Developmental Biology (7426)
  • Ecology (11391)
  • Epidemiology (2066)
  • Evolutionary Biology (15127)
  • Genetics (10418)
  • Genomics (14029)
  • Immunology (9154)
  • Microbiology (22131)
  • Molecular Biology (8797)
  • Neuroscience (47470)
  • Paleontology (350)
  • Pathology (1423)
  • Pharmacology and Toxicology (2486)
  • Physiology (3712)
  • Plant Biology (8069)
  • Scientific Communication and Education (1434)
  • Synthetic Biology (2217)
  • Systems Biology (6023)
  • Zoology (1251)