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Structure paper

TitleX-ray structure and enzymatic study of a bacterial NADPH oxidase highlight the activation mechanism of eukaryotic NOX.
Journal, issue, pagesElife, Vol. 13, Year 2024
Publish dateOct 3, 2023 (structure data deposition date)
AuthorsPetit-Hartlein, I. / Vermot, A. / Thepaut, M. / Humm, A.S. / Dupeux, F. / Dupuy, J. / Chaptal, V. / Marquez, J.A. / Smith, S.M.E. / Fieschi, F.
External linksElife / PubMed:38640072
MethodsX-ray diffraction
Resolution1.941 - 3.62 Å
Structure data

PDB-8qq1:
SpNOX dehydrogenase domain, mutant F397W in complex with Flavin adenine dinucleotide (FAD)
Method: X-RAY DIFFRACTION / Resolution: 1.941 Å

PDB-8qq5:
Structure of WT SpNox DH domain: a bacterial NADPH oxidase.
Method: X-RAY DIFFRACTION / Resolution: 2.5 Å

PDB-8qq7:
Structure of SpNOX: a Bacterial NADPH oxidase
Method: X-RAY DIFFRACTION / Resolution: 3.62 Å

Chemicals

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

ChemComp-BR:
BROMIDE ION

ChemComp-HOH:
WATER

ChemComp-CL:
Unknown entry

ChemComp-FDA:
DIHYDROFLAVINE-ADENINE DINUCLEOTIDE

ChemComp-HEM:
PROTOPORPHYRIN IX CONTAINING FE

Source
  • streptococcus pneumoniae (bacteria)
KeywordsMEMBRANE PROTEIN / Streptococcus pneumoniae NADPH Oxidase (spNOX) Reactive oxygen species (ROS) membrane protein electron transfer oxidative stress / ELECTRON TRANSPORT / NADPH oxidase / Reactive Oxygen Species production / Dehydrogenase domain / Streptococcus pneumoniae. / Streptococcus pneumoniae / F397W mutant / electron transport.

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