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- EMDB-45849: Focused map of Ku70/80 on the active side of the ligation complex... -

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Basic information

Entry
Database: EMDB / ID: EMD-45849
TitleFocused map of Ku70/80 on the active side of the ligation complex in the NHEJ pathway
Map dataFocused map of active Ku70/80 complex in ligation complex I
Sample
  • Complex: Ligation complex in the NHEJ pathway
    • Protein or peptide: human Ku70
    • Protein or peptide: human Ku80
    • DNA: DNA chain J
    • DNA: DNA chain L
KeywordsNHEJ / ligation / XLF / PAXX / DNA repair / Ligase IV / DNA BINDING PROTEIN
Biological speciesHomo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.2 Å
AuthorsLi J / Liu L / Gellert M / Yang W
Funding support United States, 1 items
OrganizationGrant numberCountry
National Institutes of Health/National Institute of Diabetes and Digestive and Kidney Disease (NIH/NIDDK) United States
CitationJournal: Nature / Year: 2025
Title: Dynamic assemblies and coordinated reactions of non-homologous end joining.
Authors: Lan Liu / Jun Li / Metztli Cisneros-Aguirre / Arianna Merkell / Jeremy M Stark / Martin Gellert / Wei Yang /
Abstract: Non-homologous end joining (NHEJ) is the main repair pathway of double-strand DNA breaks in higher eukaryotes. Here we report reconstitution of the final steps of NHEJ and structures of DNA ...Non-homologous end joining (NHEJ) is the main repair pathway of double-strand DNA breaks in higher eukaryotes. Here we report reconstitution of the final steps of NHEJ and structures of DNA polymerase μ and ligase IV (LIG4) engaged in gap filling and end joining. These reactions take place in a flexible ω-shaped framework composed of XRCC4 and XLF. Two broken DNA ends, each encircled by Ku70-Ku80 internally, are docked onto the ω frame, mediated by LIG4. DNA polymerase and ligase attached to each ω arm repair only one broken strand of a defined polarity; the final steps of NHEJ requires coordination and toggling of a pair of such enzymes. The facilitators XLF and PAXX additively stimulate NHEJ reactions. As DNA-end sensor and protector, LIG4 replaces DNA-PKcs for end joining and bridges the two DNA ends for polymerase to fill remaining gaps. These assemblies present new targets for NHEJ inhibition to enhance efficacy of radiotherapy and accuracy of gene editing.
History
DepositionJul 21, 2024-
Header (metadata) releaseApr 23, 2025-
Map releaseApr 23, 2025-
UpdateNov 5, 2025-
Current statusNov 5, 2025Processing site: RCSB / Status: Released

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Structure visualization

Supplemental images

emd_45849.png

Downloads & links

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Map

FileDownload / File: emd_45849.map.gz / Format: CCP4 / Size: 512 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
AnnotationFocused map of active Ku70/80 complex in ligation complex I
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
0.83 Å/pix.
x 512 pix.
= 426.496 Å		0.83 Å/pix.
x 512 pix.
= 426.496 Å		0.83 Å/pix.
x 512 pix.
= 426.496 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 0.833 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.25
Minimum - Maximum-0.48778474 - 1.2134267
Average (Standard dev.)-0.0011027376 (±0.020960713)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions512512512
Spacing512512512
CellA=B=C: 426.496 Å
α=β=γ: 90.0 °

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Supplemental data

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Mask #1

Fileemd_45849_msk_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: half 2 map

Fileemd_45849_half_map_1.map
Annotationhalf 2 map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: half 1 map

Fileemd_45849_half_map_2.map
Annotationhalf 1 map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Sample components

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Entire : Ligation complex in the NHEJ pathway

EntireName: Ligation complex in the NHEJ pathway
Components
  • Complex: Ligation complex in the NHEJ pathway
    • Protein or peptide: human Ku70
    • Protein or peptide: human Ku80
    • DNA: DNA chain J
    • DNA: DNA chain L

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Supramolecule #1: Ligation complex in the NHEJ pathway

SupramoleculeName: Ligation complex in the NHEJ pathway / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 854 KDa

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Macromolecule #1: human Ku70

MacromoleculeName: human Ku70 / type: protein_or_peptide / ID: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: GPVMSGWESY YKTEGDEEAE EEQEENLEAS GDYKYSGRDS LIFLVDASKA MFESQSEDEL TPF DMSIQC IQSVYISKII SSDRDLLAVV FYGTEKDKNS VNFKNIYVLQ ELDNPGAKRI LELD QFKGQ QGQKRFQDMM GHGSDYSLSE VLWVCANLFS DVQFKMSHKR ...String:
GPVMSGWESY YKTEGDEEAE EEQEENLEAS GDYKYSGRDS LIFLVDASKA MFESQSEDEL TPF DMSIQC IQSVYISKII SSDRDLLAVV FYGTEKDKNS VNFKNIYVLQ ELDNPGAKRI LELD QFKGQ QGQKRFQDMM GHGSDYSLSE VLWVCANLFS DVQFKMSHKR IMLFTNEDNP HGNDS AKAS RARTKAGDLR DTGIFLDLMH LKKPGGFDIS LFYRDIISIA EDEDLRVHFE ESSKLE DLL RKVRAKETRK RALSRLKLKL NKDIVISVGI YNLVQKALKP PPIKLYRETN EPVKTKT RT FNTSTGGLLL PSDTKRSQIY GSRQIILEKE ETEELKRFDD PGLMLMGFKP LVLLKKHH Y LRPSLFVYPE ESLVIGSSTL FSALLIKCLE KEVAALCRYT PRRNIPPYFV ALVPQEEEL DDQKIQVTPP GFQLVFLPFA DDKRKMPFTE KIMATPEQVG KMKAIVEKLR FTYRSDSFEN PVLQQHFRN LEALALDLME PEQAVDLTLP KVEAMNKRLG SLVDEFKELV YPPDYNPEGK V TKRKHDNE GSGSKRPKVE YSEEELKTHI SKGTLGKFTV PMLKEACRAY GLKSGLKKQE LL EALTKHF QD

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Macromolecule #2: human Ku80

MacromoleculeName: human Ku80 / type: protein_or_peptide / ID: 2 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: MVRSGNKAAV VLCMDVGFTM SNSIPGIESP FEQAKKVITM FVQRQVFAEN KDEIALVLFG TDGTDNPLS GGDQYQNITV HRHLMLPDFD LLEDIESKIQ PGSQQADFLD ALIVSMDVIQ H ETIGKKFE KRHIEIFTDL SSRFSKSQLD IIIHSLKKCD ISLQFFLPFS ...String:
MVRSGNKAAV VLCMDVGFTM SNSIPGIESP FEQAKKVITM FVQRQVFAEN KDEIALVLFG TDGTDNPLS GGDQYQNITV HRHLMLPDFD LLEDIESKIQ PGSQQADFLD ALIVSMDVIQ H ETIGKKFE KRHIEIFTDL SSRFSKSQLD IIIHSLKKCD ISLQFFLPFS LGKEDGSGDR GD GPFRLGG HGPSFPLKGI TEQQKEGLEI VKMVMISLEG EDGLDEIYSF SESLRKLCVF KKI ERHSIH WPCRLTIGSN LSIRIAAYKS ILQERVKKTW TVVDAKTLKK EDIQKETVYC LNDD DETEV LKEDIIQGFR YGSDIVPFSK VDEEQMKYKS EGKCFSVLGF CKSSQVQRRF FMGNQ VLKV FAARDDEAAA VALSSLIHAL DDLDMVAIVR YAYDKRANPQ VGVAFPHIKH NYECLV YVQ LPFMEDLRQY MFSSLKNSKK YAPTEAQLNA VDALIDSMSL AKKDEKTDTL EDLFPTT KI PNPRFQRLFQ CLLHRALHPR EPLPPIQQHI WNMLNPPAEV TTKSQIPLSK IKTLFPLI E AKKKDQVTAQ EIFQDNHEDG PTAKKLKTEQ GGAHFSVSSL AEGSVTSVGS VNPAENFRV LVKQKKASFE EASNQLINHI EQFLDTNETP YFMKSIDCIR AFREEAIKFS EEQRFNNFLK ALQEKVEIK QLNHFWEIVV QDGITLITKE EASGSSVTAE EAKKFLAPKD KPSGDTAAVF E EGGDVDDL LDMI

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Macromolecule #3: DNA chain J

MacromoleculeName: DNA chain J / type: dna / ID: 3 / Classification: DNA
Source (natural)Organism: Homo sapiens (human)
SequenceString:
CGCGCCCAGC TTTCCCAGCT AATAAACTAA AAACATTCGT TCACGTGAGT TCCAGTACAA GTCTGGTC

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Macromolecule #4: DNA chain L

MacromoleculeName: DNA chain L / type: dna / ID: 4 / Classification: DNA
Source (natural)Organism: Homo sapiens (human)
SequenceString:
AGACTTGTAC TGGAACTCAC GTGAACGAAT GTTTTTAGTT TATTGGGCGC G

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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

Concentration0.35 mg/mL
BufferpH: 7.9
VitrificationCryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 277 K

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Electron microscopy

MicroscopeFEI TITAN KRIOS
Image recordingFilm or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Average electron dose: 42.2 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 1.5 µm / Nominal defocus min: 0.5 µm
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
Startup modelType of model: EMDB MAP
EMDB ID:

23509

Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.2 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 500830
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD
FSC plot (resolution estimation)

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