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TitleInsights into the structure-function relationship of the NorQ/NorD chaperones from Paracoccus denitrificans reveal shared principles of interacting MoxR AAA+/VWA domain proteins.
Journal, issue, pagesBMC Biol, Vol. 21, Issue 1, Page 47, Year 2023
Publish dateFeb 28, 2023
AuthorsMaximilian Kahle / Sofia Appelgren / Arne Elofsson / Marta Carroni / Pia Ädelroth /
PubMed AbstractBACKGROUND: NorQ, a member of the MoxR-class of AAA+ ATPases, and NorD, a protein containing a Von Willebrand Factor Type A (VWA) domain, are essential for non-heme iron (Fe) cofactor insertion into ...BACKGROUND: NorQ, a member of the MoxR-class of AAA+ ATPases, and NorD, a protein containing a Von Willebrand Factor Type A (VWA) domain, are essential for non-heme iron (Fe) cofactor insertion into cytochrome c-dependent nitric oxide reductase (cNOR). cNOR catalyzes NO reduction, a key step of bacterial denitrification. This work aimed at elucidating the specific mechanism of NorQD-catalyzed Fe insertion, and the general mechanism of the MoxR/VWA interacting protein families.
RESULTS: We show that NorQ-catalyzed ATP hydrolysis, an intact VWA domain in NorD, and specific surface carboxylates on cNOR are all features required for cNOR activation. Supported by BN-PAGE, low-resolution cryo-EM structures of NorQ and the NorQD complex show that NorQ forms a circular hexamer with a monomer of NorD binding both to the side and to the central pore of the NorQ ring. Guided by AlphaFold predictions, we assign the density that "plugs" the NorQ ring pore to the VWA domain of NorD with a protruding "finger" inserting through the pore and suggest this binding mode to be general for MoxR/VWA couples.
CONCLUSIONS: Based on our results, we present a tentative model for the mechanism of NorQD-catalyzed cNOR remodeling and suggest many of its features to be applicable to the whole MoxR/VWA family.
External linksBMC Biol / PubMed:36855050 / PubMed Central
MethodsEM (single particle)
Resolution5.09 - 7.82 Å
Structure data

EMDB-16655: Low-resolution cryo-EM structure of the NorQD chaperone complex from Paracoccus denitrificans
Method: EM (single particle) / Resolution: 5.09 Å

EMDB-16656: Low-resolution structure of the NorQ chaperone from Paracoccus denitrificans
Method: EM (single particle) / Resolution: 7.82 Å

Source
  • Paracoccus denitrificans (bacteria)

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