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Structure paper

TitleStructural basis of human NOX5 activation.
Journal, issue, pagesNat Commun, Vol. 15, Issue 1, Page 3994, Year 2024
Publish dateMay 11, 2024
AuthorsChenxi Cui / Meiqin Jiang / Nikhil Jain / Sourav Das / Yu-Hua Lo / Ali A Kermani / Tanadet Pipatpolkai / Ji Sun /
PubMed AbstractNADPH oxidase 5 (NOX5) catalyzes the production of superoxide free radicals and regulates physiological processes from sperm motility to cardiac rhythm. Overexpression of NOX5 leads to cancers, ...NADPH oxidase 5 (NOX5) catalyzes the production of superoxide free radicals and regulates physiological processes from sperm motility to cardiac rhythm. Overexpression of NOX5 leads to cancers, diabetes, and cardiovascular diseases. NOX5 is activated by intracellular calcium signaling, but the underlying molecular mechanism of which - in particular, how calcium triggers electron transfer from NADPH to FAD - is still unclear. Here we capture motions of full-length human NOX5 upon calcium binding using single-particle cryogenic electron microscopy (cryo-EM). By combining biochemistry, mutagenesis analyses, and molecular dynamics (MD) simulations, we decode the molecular basis of NOX5 activation and electron transfer. We find that calcium binding to the EF-hand domain increases NADPH dynamics, permitting electron transfer between NADPH and FAD and superoxide production. Our structural findings also uncover a zinc-binding motif that is important for NOX5 stability and enzymatic activity, revealing modulation mechanisms of reactive oxygen species (ROS) production.
External linksNat Commun / PubMed:38734761 / PubMed Central
MethodsEM (single particle)
Resolution3.2 - 4.06 Å
Structure data

42013

8u7y

EMDB-42013, PDB-8u7y:
Structural Basis of Human NOX5 Activation
Method: EM (single particle) / Resolution: 4.06 Å

42014

8u85

EMDB-42014, PDB-8u85:
Structural Basis of Human NOX5 Activation
Method: EM (single particle) / Resolution: 3.2 Å

42015

8u86

EMDB-42015, PDB-8u86:
Structural Basis of Human NOX5 Activation
Method: EM (single particle) / Resolution: 3.3 Å

42016

8u87

EMDB-42016, PDB-8u87:
Structural Basis of Human NOX5 Activation
Method: EM (single particle) / Resolution: 3.86 Å

Chemicals

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

ChemComp-D12:
DODECANE

ChemComp-D10:
DECANE

ChemComp-NAP:
NADP NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE

ChemComp-HEB:
HEME B/C

ChemComp-ZN:
Unknown entry

ChemComp-NDP:
NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE

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

Source
  • homo sapiens (human)
KeywordsMEMBRANE PROTEIN / enzyme / oxidase / activation mechanism

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