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- PDB-9x1l: The cryo-EM structure of HerA-NurA complex with AMPPNP from Therm... -

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Basic information

Entry
Database: PDB / ID: 9x1l
TitleThe cryo-EM structure of HerA-NurA complex with AMPPNP from Thermococcus kodakarensis
Components
  • 5'-3' nuclease, encoded next to Rad50 and Mre11 homologs
  • DNA helicase
KeywordsTRANSLOCASE / HerA / Helicase / NurA / Nuclease
Function / homology
Function and homology information


3'-5' DNA helicase activity / 5'-3' DNA helicase activity / metal ion binding
Similarity search - Function
: / Helicase HerA, barrel domain / HAS barrel domain / DNA double-strand break repair nuclease NurA-like / : / NurA domain / NurA domain / NurA / Helicase HerA-like / Helicase HerA, central domain ...: / Helicase HerA, barrel domain / HAS barrel domain / DNA double-strand break repair nuclease NurA-like / : / NurA domain / NurA domain / NurA / Helicase HerA-like / Helicase HerA, central domain / Helicase HerA, central domain / P-loop containing nucleoside triphosphate hydrolase
Similarity search - Domain/homology
PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER / 5'-3' nuclease, encoded next to Rad50 and Mre11 homologs / Bipolar DNA helicase
Similarity search - Component
Biological speciesThermococcus kodakarensis (archaea)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 2.8 Å
AuthorsUda, K. / Numata, T.
Funding support Japan, 5items
OrganizationGrant numberCountry
Japan Society for the Promotion of Science (JSPS)JP19K22289 Japan
Japan Society for the Promotion of Science (JSPS)JP21K05394 Japan
Japan Society for the Promotion of Science (JSPS)20H02916 Japan
Japan Society for the Promotion of Science (JSPS)20K21281 Japan
Japan Society for the Promotion of Science (JSPS)24H00505 Japan
CitationJournal: To Be Published
Title: Substrate specificity and mechanism of action of the HerA-NurA nuclease from the hyperthermophilic archaeon Thermococcus kodakarensis
Authors: Uda, K. / Numata, T.
History
DepositionOct 2, 2025Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Feb 4, 2026Provider: repository / Type: Initial release
Revision 1.0Feb 4, 2026Data content type: EM metadata / Data content type: EM metadata / Provider: repository / Type: Initial release
Revision 1.0Feb 4, 2026Data content type: Additional map / Part number: 1 / Data content type: Additional map / Provider: repository / Type: Initial release
Revision 1.0Feb 4, 2026Data content type: FSC / Data content type: FSC / Provider: repository / Type: Initial release
Revision 1.0Feb 4, 2026Data content type: Half map / Part number: 1 / Data content type: Half map / Provider: repository / Type: Initial release
Revision 1.0Feb 4, 2026Data content type: Half map / Part number: 2 / Data content type: Half map / Provider: repository / Type: Initial release
Revision 1.0Feb 4, 2026Data content type: Image / Data content type: Image / Provider: repository / Type: Initial release
Revision 1.0Feb 4, 2026Data content type: Mask / Part number: 1 / Data content type: Mask / Provider: repository / Type: Initial release
Revision 1.0Feb 4, 2026Data content type: Primary map / Data content type: Primary map / Provider: repository / Type: Initial release

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

Downloads & links

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Assembly

Deposited unit
A: DNA helicase
B: DNA helicase
C: DNA helicase
D: DNA helicase
E: DNA helicase
F: DNA helicase
G: 5'-3' nuclease, encoded next to Rad50 and Mre11 homologs
H: 5'-3' nuclease, encoded next to Rad50 and Mre11 homologs
hetero molecules


Theoretical massNumber of molelcules
Total (without water)501,81714
Polymers498,7808
Non-polymers3,0376
Water00
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: electron microscopy, not applicable
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1

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Components

#1: Protein
DNA helicase


Mass: 66118.117 Da / Num. of mol.: 6
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Thermococcus kodakarensis (archaea) / Gene: TK2213 / Plasmid: pET24(a) / Production host: Escherichia coli BL21(DE3) (bacteria) / Variant (production host): Gold CodonPlus RIL / References: UniProt: Q5JHP7, DNA helicase
#2: Protein 5'-3' nuclease, encoded next to Rad50 and Mre11 homologs


Mass: 51035.672 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Thermococcus kodakarensis (archaea) / Gene: TK2210 / Plasmid: pET21a / Production host: Escherichia coli BL21(DE3) (bacteria) / Variant (production host): Gold CodonPlus RIL / References: UniProt: Q5JHL5
#3: Chemical
ChemComp-ANP / PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER


Mass: 506.196 Da / Num. of mol.: 6 / Source method: obtained synthetically / Formula: C10H17N6O12P3 / Feature type: SUBJECT OF INVESTIGATION / Comment: AMP-PNP, energy-carrying molecule analogue*YM
Has ligand of interestY
Has protein modificationN

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Experimental details

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Experiment

ExperimentMethod: ELECTRON MICROSCOPY
EM experimentAggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction

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Sample preparation

ComponentName: Thermococcus kodakarensis HerA-NurA complex / Type: COMPLEX / Entity ID: #1-#2 / Source: RECOMBINANT
Molecular weightValue: 0.5 MDa / Experimental value: NO
Source (natural)Organism: Thermococcus kodakarensis (archaea)
Source (recombinant)Organism: Escherichia coli BL21(DE3) (bacteria) / Strain: Gold CodonPlus RIL / Plasmid: pET21a, pET24a
Buffer solutionpH: 7
Buffer component
IDConc.NameBuffer-ID
1100 mMsodium chloride1
22.5 mMmanganese chloride1
31 mMAMPPNP1
40.001 %LMNG1
550 mMTris-HCl1
SpecimenConc.: 4 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
Specimen supportGrid material: COPPER / Grid mesh size: 300 divisions/in. / Grid type: Quantifoil R1.2/1.3
VitrificationInstrument: FEI VITROBOT MARK IV / Cryogen name: ETHANE / Humidity: 100 % / Chamber temperature: 281 K

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Electron microscopy imaging

MicroscopyModel: JEOL CRYO ARM 300
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM
Electron lensMode: BRIGHT FIELD / Nominal magnification: 60000 X / Nominal defocus max: 1600 nm / Nominal defocus min: 1400 nm / Cs: 2.7 mm / C2 aperture diameter: 70 µm
Specimen holderCryogen: NITROGEN
Image recordingAverage exposure time: 2.5 sec. / Electron dose: 50 e/Å2 / Film or detector model: GATAN K3 (6k x 4k) / Num. of grids imaged: 1 / Num. of real images: 4750
EM imaging opticsEnergyfilter name: In-column Omega Filter

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Processing

EM software
IDNameVersionCategory
1cryoSPARCparticle selection
2Topazparticle selection
3SerialEMimage acquisition
5cryoSPARCCTF correction
8UCSF Chimeramodel fitting
9UCSF ChimeraXmodel fitting
10PHENIXmodel fitting
12PHENIX1.19.2_4158model refinement
13Cootmodel refinement
14cryoSPARCinitial Euler assignment
15cryoSPARCfinal Euler assignment
16cryoSPARCclassification
17cryoSPARC3D reconstruction
CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
SymmetryPoint symmetry: C2 (2 fold cyclic)
3D reconstructionResolution: 2.8 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 204172 / Symmetry type: POINT
Atomic model buildingSource name: AlphaFold / Type: in silico model
RefinementHighest resolution: 2.8 Å
Stereochemistry target values: REAL-SPACE (WEIGHTED MAP SUM AT ATOM CENTERS)
Refine LS restraints
Refine-IDTypeDev idealNumber
ELECTRON MICROSCOPYf_bond_d0.00334538
ELECTRON MICROSCOPYf_angle_d0.44846678
ELECTRON MICROSCOPYf_dihedral_angle_d10.513066
ELECTRON MICROSCOPYf_chiral_restr0.0425190
ELECTRON MICROSCOPYf_plane_restr0.0046014

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