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Structure paper

TitleStructure of human phagocyte NADPH oxidase in the resting state.
Journal, issue, pagesElife, Vol. 11, Year 2022
Publish dateNov 22, 2022
AuthorsRui Liu / Kangcheng Song / Jing-Xiang Wu / Xiao-Peng Geng / Liming Zheng / Xiaoyin Gao / Hailin Peng / Lei Chen /
PubMed AbstractPhagocyte 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 that ...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 that participate in pathogen killing. The resting phagocyte oxidase is a heterodimeric complex formed by two transmembrane proteins NOX2 and p22. Despite the physiological importance of this complex, its structure remains elusive. Here, we reported the cryo-EM structure of the functional human NOX2-p22 complex in nanodisc in the resting state. NOX2 shows a canonical 6-TM architecture of NOX and p22 has four transmembrane helices. M3, M4, and M5 of NOX2, and M1 and M4 helices of p22 are involved in the heterodimer formation. Dehydrogenase (DH) domain of NOX2 in the resting state is not optimally docked onto the transmembrane domain, leading to inefficient electron transfer and NADPH binding. Structural analysis suggests that the cytosolic factors might activate the NOX2-p22 complex by stabilizing the DH in a productive docked conformation.
External linksElife / PubMed:36413210 / PubMed Central
MethodsEM (single particle)
Resolution2.8 - 3.3 Å
Structure data

34389

8gz3

EMDB-34389, PDB-8gz3:
Structure of human phagocyte NADPH oxidase in the resting state
Method: EM (single particle) / Resolution: 3.3 Å

EMDB-34390: Consensus map of human phagocyte NADPH oxidase in the resting state
Method: EM (single particle) / Resolution: 3.3 Å

EMDB-34620: Focus refined map of the constant regions of Fab heavy chain and light chain and TP1170 of human phagocyte NADPH oxidase in the resting state
Method: EM (single particle) / Resolution: 3.1 Å

EMDB-34621: Focus refined map of human phagocyte NADPH oxidase core in the resting state
Method: EM (single particle) / Resolution: 2.8 Å

EMDB-34622: Focus refined map of the DH domain of human phagocyte NADPH oxidase in the resting state
Method: EM (single particle) / Resolution: 3.1 Å

Chemicals

ChemComp-FAD:
FLAVIN-ADENINE DINUCLEOTIDE / FAD*YM

ChemComp-HEM:
PROTOPORPHYRIN IX CONTAINING FE

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose

ChemComp-LBN:
1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine / phospholipid*YM

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
  • mus musculus (house mouse)
  • vicugna pacos (alpaca)
KeywordsOXIDOREDUCTASE / NOX2 / p22 / CYBA / CYBB / TP1170 / NOX

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