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TitleStructures of mouse DUOX1-DUOXA1 provide mechanistic insights into enzyme activation and regulation.
Journal, issue, pagesNat Struct Mol Biol, Vol. 27, Issue 11, Page 1086-1093, Year 2020
Publish dateSep 14, 2020
AuthorsJi Sun /
PubMed AbstractDUOX1, an NADPH oxidase family member, catalyzes the production of hydrogen peroxide. DUOX1 is expressed in various tissues, including the thyroid and respiratory tract, and plays a crucial role in ...DUOX1, an NADPH oxidase family member, catalyzes the production of hydrogen peroxide. DUOX1 is expressed in various tissues, including the thyroid and respiratory tract, and plays a crucial role in processes such as thyroid hormone biosynthesis and innate host defense. DUOX1 co-assembles with its maturation factor DUOXA1 to form an active enzyme complex. However, the molecular mechanisms for activation and regulation of DUOX1 remain mostly unclear. Here, I present cryo-EM structures of the mammalian DUOX1-DUOXA1 complex, in the absence and presence of substrate NADPH, as well as DUOX1-DUOXA1 in an unexpected dimer-of-dimers configuration. These structures reveal atomic details of the DUOX1-DUOXA1 interaction, a lipid-mediated NADPH-binding pocket and the electron transfer path. Furthermore, biochemical and structural analyses indicate that the dimer-of-dimers configuration represents an inactive state of DUOX1-DUOXA1, suggesting an oligomerization-dependent regulatory mechanism. Together, my work provides structural bases for DUOX1-DUOXA1 activation and regulation.
External linksNat Struct Mol Biol / PubMed:32929281 / PubMed Central
MethodsEM (single particle)
Resolution2.7 - 3.3 Å
Structure data

21962

6wxr

EMDB-21962, PDB-6wxr:
CryoEM structure of mouse DUOX1-DUOXA1 complex in the absence of NADPH
Method: EM (single particle) / Resolution: 3.2 Å

21963

6wxu

EMDB-21963, PDB-6wxu:
CryoEM structure of mouse DUOX1-DUOXA1 complex in the dimer-of-dimer state
Method: EM (single particle) / Resolution: 2.7 Å

21964

6wxv

EMDB-21964, PDB-6wxv:
CryoEM structure of mouse DUOX1-DUOXA1 complex in the presence of NADPH
Method: EM (single particle) / Resolution: 3.3 Å

Chemicals

ChemComp-FAD:
FLAVIN-ADENINE DINUCLEOTIDE / FAD*YM / Flavin adenine dinucleotide

ChemComp-NAG:
2-acetamido-2-deoxy-beta-D-glucopyranose / N-Acetylglucosamine

ChemComp-HEM:
PROTOPORPHYRIN IX CONTAINING FE / Heme B

ChemComp-HEC:
HEME C / Heme C

ChemComp-PX2:
1,2-DILAUROYL-SN-GLYCERO-3-PHOSPHATE

ChemComp-PLC:
DIUNDECYL PHOSPHATIDYL CHOLINE / phospholipid*YM

ChemComp-HEB:
HEME B/C

ChemComp-NDP:
NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE / Nicotinamide adenine dinucleotide phosphate

ChemComp-CA:
Unknown entry

Source
  • mus musculus (house mouse)
KeywordsMEMBRANE PROTEIN / NADPH oxidase / ROS production / protein complex

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