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- EMDB-53163: NorQD complex state 4 from Jhaorihella thermophila -

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Basic information

Entry
Database: EMDB / ID: EMD-53163
TitleNorQD complex state 4 from Jhaorihella thermophila
Map datamain map
Sample
  • Complex: NorQD complex from J. thermophila
    • Protein or peptide: Nitric oxide reductase NorQ protein
    • Protein or peptide: Nitric oxide reductase NorD protein
  • Ligand: ADENOSINE-5'-TRIPHOSPHATE
  • Ligand: ADENOSINE-5'-DIPHOSPHATE
KeywordsAAA+ Protein / MoxR / VWA domain / Nitric Oxide Reductase / CHAPERONE
Function / homology
Function and homology information


ATP hydrolysis activity / ATP binding
Similarity search - Function
: / CbbQ/NirQ/NorQ, C-terminal / CbbQ/NirQ/NorQ C-terminal / : / ATPase, dynein-related, AAA domain / AAA domain (dynein-related subfamily) / von Willebrand factor type A domain / VWFA domain profile. / von Willebrand factor (vWF) type A domain / von Willebrand factor, type A ...: / CbbQ/NirQ/NorQ, C-terminal / CbbQ/NirQ/NorQ C-terminal / : / ATPase, dynein-related, AAA domain / AAA domain (dynein-related subfamily) / von Willebrand factor type A domain / VWFA domain profile. / von Willebrand factor (vWF) type A domain / von Willebrand factor, type A / von Willebrand factor A-like domain superfamily / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
Nitric oxide reductase NorQ protein / Nitric oxide reductase NorD protein
Similarity search - Component
Biological speciesJhaorihella thermophila (bacteria)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.9 Å
AuthorsKahle M / Appelgren S / Carroni M / Adelroth P / Wendler P
Funding support Germany, Sweden, 2 items
OrganizationGrant numberCountry
German Research Foundation (DFG) Germany
Swedish Research Council Sweden
CitationJournal: Nat Commun / Year: 2026
Title: NorQD AAA+ complex drives metal insertion by a twisting mechanism.
Authors: Maximilian Kahle / Sofia Appelgren / Finja König / Marta Carroni / Pia Ädelroth / Petra Wendler /
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.
History
DepositionMar 15, 2025-
Header (metadata) releaseMar 25, 2026-
Map releaseMar 25, 2026-
UpdateMay 13, 2026-
Current statusMay 13, 2026Processing site: PDBe / Status: Released

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Structure visualization

Supplemental images

emd_53163.png

Downloads & links

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Map

FileDownload / File: emd_53163.map.gz / Format: CCP4 / Size: 91.1 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Annotationmain map
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
0.85 Å/pix.
x 288 pix.
= 243.648 Å		0.85 Å/pix.
x 288 pix.
= 243.648 Å		0.85 Å/pix.
x 288 pix.
= 243.648 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 0.846 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.09
Minimum - Maximum-0.18746217 - 0.40196168
Average (Standard dev.)0.001145104 (±0.018445143)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions288288288
Spacing288288288
CellA=B=C: 243.64801 Å
α=β=γ: 90.0 °

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Supplemental data

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Mask #1

Fileemd_53163_msk_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Additional map: shapened map

Fileemd_53163_additional_1.map
Annotationshapened map
Projections & Slices
AxesZYX

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Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: half map 1

Fileemd_53163_half_map_1.map
Annotationhalf map 1
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: half map 2

Fileemd_53163_half_map_2.map
Annotationhalf map 2
Projections & Slices
AxesZYX

Projections

Slices (1/2)
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Histogram

Histogram (log scale)

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Sample components

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Entire : NorQD complex from J. thermophila

EntireName: NorQD complex from J. thermophila
Components
  • Complex: NorQD complex from J. thermophila
    • Protein or peptide: Nitric oxide reductase NorQ protein
    • Protein or peptide: Nitric oxide reductase NorD protein
  • Ligand: ADENOSINE-5'-TRIPHOSPHATE
  • Ligand: ADENOSINE-5'-DIPHOSPHATE

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Supramolecule #1: NorQD complex from J. thermophila

SupramoleculeName: NorQD complex from J. thermophila / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#2
Source (natural)Organism: Jhaorihella thermophila (bacteria)
Molecular weightTheoretical: 258 KDa

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Macromolecule #1: Nitric oxide reductase NorQ protein

MacromoleculeName: Nitric oxide reductase NorQ protein / type: protein_or_peptide / ID: 1 / Number of copies: 6 / Enantiomer: LEVO
Source (natural)Organism: Jhaorihella thermophila (bacteria)
Molecular weightTheoretical: 29.382672 KDa
Recombinant expressionOrganism: Escherichia coli BL21(DE3) (bacteria)
SequenceString: MDGSTTFGGA ATAPFYLPQA DECEVFAAAH ENDLPVLLKG PTGCGKTRFV AHMAQRLGRK LYTVACHDDL AAADLIGRYL LKGGETVWV DGPLTRAVRE GAICYLDQVV EARKDVTVVL HPLTDDRRIL PIDRTGEELE AAPGFMLVAS YNPGYQNILK T LKPSTRQR ...String:
MDGSTTFGGA ATAPFYLPQA DECEVFAAAH ENDLPVLLKG PTGCGKTRFV AHMAQRLGRK LYTVACHDDL AAADLIGRYL LKGGETVWV DGPLTRAVRE GAICYLDQVV EARKDVTVVL HPLTDDRRIL PIDRTGEELE AAPGFMLVAS YNPGYQNILK T LKPSTRQR FISIEFDFPH PDLETEVVAQ ESGLPLERCK PLIRLANKLR ALKGQDLEEG VSTRLVVYAA TLIAQGMNTD RA IRAAMIE PLTDDEDVKR GLLDLVTAVF G

UniProtKB: Nitric oxide reductase NorQ protein

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Macromolecule #2: Nitric oxide reductase NorD protein

MacromoleculeName: Nitric oxide reductase NorD protein / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Jhaorihella thermophila (bacteria)
Molecular weightTheoretical: 71.726891 KDa
Recombinant expressionOrganism: Escherichia coli BL21(DE3) (bacteria)
SequenceString: MDRIEFEPWE PEETVGKLWH KFASRLDAPE AHEGAAVDLS EIGGRLAVLF RGLGGASSVE LRPVSPEISR HRLSWRRRLG AEAEAVPRA SFDGEVLRLP DRLAVFPSRE ANGALYVWLA ACAAHASDRV DQDDPLRADL AALAASRAMV AATLEDAPGL R PLYEGLCA ...String:
MDRIEFEPWE PEETVGKLWH KFASRLDAPE AHEGAAVDLS EIGGRLAVLF RGLGGASSVE LRPVSPEISR HRLSWRRRLG AEAEAVPRA SFDGEVLRLP DRLAVFPSRE ANGALYVWLA ACAAHASDRV DQDDPLRADL AALAASRAMV AATLEDAPGL R PLYEGLCA ALLHQRRVPD LPRDEAAVEA VIRNMLGDPA PLSDRAAAFQ AACAGDPLDP AITAPRKYRP FRPVPLWPEL RP VEFSEAG EVETREIEGT PEEAGEKTHR ARRRKSDQAE RRDSLILHKF EAILSWAEFL NLNRRVDDDD PDNAKKAADD QEE IGLGQI SKAPPTRLKL HLDLAPEDVD RERLSGRITY PEWDTRTGAY LPDHVCVLTS DVEAKPEQEA YAHDPAASRR IRAV RRQFE ALRPGRVTTR GHLDGDDLDI EAAVRAEVDR LASGEGSERI WLRSRPEARD LAVSILLDVS RSTESAVSGR AVIDI EREA LDALAWGLDA CGDDFAIHAF SSLKRHRVHV QRCKGFDEPM GPEVERRIGG LRPGFYTRLG AAIRHVSAEL SQQARK RRL LLVITDGKPN DLDHYEGRHG IEDTAMAVRE ARRAGHSVFG ITVDAKGKAW FSRMFGQGGF AVIPDPEKLI FALPQIY RQ LVGA

UniProtKB: Nitric oxide reductase NorD protein

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Macromolecule #3: ADENOSINE-5'-TRIPHOSPHATE

MacromoleculeName: ADENOSINE-5'-TRIPHOSPHATE / type: ligand / ID: 3 / Number of copies: 3 / Formula: ATP
Molecular weightTheoretical: 507.181 Da
Chemical component information

ChemComp-ATP:
ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying molecule*YM

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Macromolecule #4: ADENOSINE-5'-DIPHOSPHATE

MacromoleculeName: ADENOSINE-5'-DIPHOSPHATE / type: ligand / ID: 4 / Number of copies: 2 / Formula: ADP
Molecular weightTheoretical: 427.201 Da
Chemical component information

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

Concentration1 mg/mL
BufferpH: 8 / Details: 50mM TRIS/HCl,150mM KCl
GridModel: C-flat-2/2 / Material: COPPER / Mesh: 400 / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Time: 60 sec. / Pretreatment - Atmosphere: AIR / Pretreatment - Pressure: 0.05 kPa / Details: PELCO easiGlow at 20mA
VitrificationCryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 277 K / Instrument: FEI VITROBOT MARK IV

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Electron microscopy

MicroscopeTFS KRIOS
SoftwareName: EPU
Image recordingFilm or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Average electron dose: 45.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsC2 aperture diameter: 70.0 µm / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 2.5 µm / Nominal defocus min: 0.5 µm / Nominal magnification: 105000
Sample stageSpecimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

CTF correctionSoftware - Name: RELION / Type: PHASE FLIPPING AND AMPLITUDE CORRECTION
Startup modelType of model: OTHER / Details: SGD
Final reconstructionApplied symmetry - Point group: C1 (asymmetric) / Algorithm: BACK PROJECTION / Resolution.type: BY AUTHOR / Resolution: 3.9 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: cryoSPARC / Number images used: 27462
Initial angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: RELION
Final angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: RELION
FSC plot (resolution estimation)

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Atomic model buiding 1

Initial modelChain - Source name: AlphaFold / Chain - Initial model type: in silico model
SoftwareName: UCSF ChimeraX
RefinementSpace: REAL / Protocol: FLEXIBLE FIT
Output model

PDB-9qhg:
NorQD complex state 4 from Jhaorihella thermophila

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