9QHD

NorQD complex state 1 from Jhaorihella thermophila

Summary for 9QHD

• Entry DOI: 10.2210/pdb9qhd/pdb
• EMDB information: 53160
• Descriptor: Nitric oxide reductase NorQ protein, Nitric oxide reductase NorD protein, ADENOSINE-5'-TRIPHOSPHATE, ... (4 entities in total)
• Functional Keywords: aaa+ protein, moxr, vwa domain, nitric oxide reductase, chaperone
• Biological source: Jhaorihella thermophila; More
• Total number of polymer chains: 7
• Total formula weight: 250398.87

Authors

Kahle, M.,Appelgren, S.,Carroni, M.,Adelroth, P.,Wendler, P. (deposition date: 2025-03-15, release date: 2026-03-25, Last modification date: 2026-05-13)

Primary citation

Kahle, M.,Appelgren, S.,Konig, F.,Carroni, M.,Adelroth, P.,Wendler, P.
NorQD AAA+ complex drives metal insertion by a twisting mechanism.
Nat Commun, 17:-, 2026

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 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.

PubMed: 41896537
DOI: 10.1038/s41467-026-71044-4

Experimental method

ELECTRON MICROSCOPY (3.3 Å)