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NorQD AAA+ complex drives metal insertion by a twisting mechanism
Maximilian Kahle1,2, Sofia Appelgren2,3, Finja König2
1Institute of Biochemistry and Biology, Department of Biochemistry, University of Potsdam, Potsdam-Golm, Germany.
Nature Communications
|March 28, 2026
Summary
The bacterial AAA+ ATPase NorQ and its partner NorD use specific interfaces to remodel NorD, enabling metal insertion essential for nitric oxide reductase activity.
Area of Science:
- Biochemistry
- Structural Biology
- Molecular Mechanisms
Background:
- ATPases associated with diverse cellular activities (AAA+ ATPases) are crucial for various cellular processes.
- MoxR-like AAA+ ATPases often partner with VWA domain proteins for target remodeling and metal ion insertion.
- The precise mechanism of MoxR-like AAA+ ATPases, like NorQ, remains poorly understood.
Purpose of the Study:
- To elucidate the mechanism of the bacterial AAA+ ATPase NorQ in complex with its VWA domain partner NorD.
- To understand how the NorQ-NorD complex facilitates nitric oxide reductase (NOR) activity.
Main Methods:
- Cryo-electron microscopy (cryo-EM) to determine complex structures.
- Biochemical analyses to investigate protein interactions and function.
Main Results:
- Two key interaction interfaces between NorQ and NorD were identified: a VWA domain extension and the NorD C-terminus.
- NorQ was shown to remodel a critical linker region in NorD.
- This remodeling is essential for enabling metal insertion into the target NOR.
Conclusions:
- The NorQ-NorD complex utilizes specific interfaces to mediate target remodeling.
- A model is proposed where NorQ applies mechanical force to NorD, facilitating metal insertion for NOR function.
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