Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	NorQD AAA+ complex drives metal insertion by a twisting mechanism.
Journal, issue, pages	Nat Commun, Vol. 17, Issue 1, Year 2026
Publish date	Mar 27, 2026
Authors	Maximilian Kahle / Sofia Appelgren / Finja König / Marta Carroni / Pia Ädelroth / Petra Wendler /
PubMed Abstract	ATPases associated with diverse cellular activities (AAA+ -ATPases) catalyse a wide range of remodelling events in all phyla. AAA+ -ATPases of the MoxR-like family typically co-operate with von ...ATPases associated with diverse cellular activities (AAA+ -ATPases) catalyse a wide range of remodelling events in all phyla. AAA+ -ATPases of the MoxR-like family typically co-operate with von Willebrand factor type A (VWA) domain containing proteins to facilitate target remodelling and metal ion insertion, but their mechanism of action is poorly understood. We studied the bacterial AAA+ -ATPase NorQ in complex with its VWA domain partner protein NorD, which are essential for nitric oxide reductase (NOR) activity. Our cryo-EM structures and biochemical analyses show that NorQ and NorD engage through two key interfaces: (i) a finger-like extension protruding from the VWA domain that penetrates the central pore of the NorQ hexamer, and (ii) the NorD C- terminus, which contacts the post-sensor 1 loop of NorQ. Our data reveal that NorQ activity remodels a linker region in NorD essential for metal insertion. Together, these findings support a model in which the NorQ complex exerts a twisting and stretching force on the NorD linker, thereby enabling metal insertion into its target NOR.
External links	Nat Commun / PubMed:41896537 / PubMed Central
Methods	EM (single particle)
Resolution	2.9 - 3.9 Å
Structure data	53154 9qh4 EMDB-53154, PDB-9qh4: NorQ hexamer from Paracoccus denitrificans Method: EM (single particle) / Resolution: 3.7 Å 53156 9qh6 EMDB-53156, PDB-9qh6: NorQ in complex with NorD VWA domain from Paracoccus denitrificans Method: EM (single particle) / Resolution: 3.2 Å 53157 9qh7 EMDB-53157, PDB-9qh7: NorQ in complex with NorD VWA domain steep staircase subset 1 from Paracoccus denitrificans Method: EM (single particle) / Resolution: 2.9 Å 53158 9qh8 EMDB-53158, PDB-9qh8: reduced NorQ-NorD VWA domain complex from Paracoccus denitrificans Method: EM (single particle) / Resolution: 3.8 Å 53159 9qh9 EMDB-53159, PDB-9qh9: NorQ in complex with NorD VWA domain steep staircase subset 2 from Paracoccus denitrificans Method: EM (single particle) / Resolution: 3.0 Å 53160 9qhd EMDB-53160, PDB-9qhd: NorQD complex state 1 from Jhaorihella thermophila Method: EM (single particle) / Resolution: 3.3 Å 53161 9qhe EMDB-53161, PDB-9qhe: NorQD complex state 2 from Jhaorihella thermophila Method: EM (single particle) / Resolution: 3.8 Å 53162 9qhf EMDB-53162, PDB-9qhf: NorQD complex state 3 from Jhaorihella thermophila Method: EM (single particle) / Resolution: 3.9 Å 53163 9qhg EMDB-53163, PDB-9qhg: NorQD complex state 4 from Jhaorihella thermophila Method: EM (single particle) / Resolution: 3.9 Å
Chemicals	ChemComp-ATP: ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying moleculeYM ChemComp-ADP: ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying moleculeYM ChemComp-MG: Unknown entry
Source	paracoccus denitrificans (bacteria) jhaorihella thermophila (bacteria)
Keywords	CHAPERONE / AAA+ protein / MoxR / VWA domain / nitric oxide reductase