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- EMDB-54481: MVV STC intasome in complex with LEDGF -

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Basic information

Entry
Database: EMDB / ID: EMD-54481
TitleMVV STC intasome in complex with LEDGF
Map data
Sample
  • Complex: MVV STC intasome in complex with LEDGF
    • Protein or peptide: Gag-Pol polyprotein
    • Protein or peptide: PC4 and SFRS1-interacting protein
    • DNA: DNA EV392
    • DNA: DNA EV306
    • DNA: DNA EV391
  • Ligand: ZINC ION
Keywordsintegrase / LEDGF / p75 / MVV / DNA / VIRAL PROTEIN
Function / homology
Function and homology information


dUTP diphosphatase / dUTP diphosphatase activity / nucleotide metabolic process / Integration of viral DNA into host genomic DNA / Autointegration results in viral DNA circles / Hydrolases; Acting on peptide bonds (peptidases); Aspartic endopeptidases / ribonuclease H / supercoiled DNA binding / 2-LTR circle formation / Vpr-mediated nuclear import of PICs ...dUTP diphosphatase / dUTP diphosphatase activity / nucleotide metabolic process / Integration of viral DNA into host genomic DNA / Autointegration results in viral DNA circles / Hydrolases; Acting on peptide bonds (peptidases); Aspartic endopeptidases / ribonuclease H / supercoiled DNA binding / 2-LTR circle formation / Vpr-mediated nuclear import of PICs / Formation of WDR5-containing histone-modifying complexes / mRNA 5'-splice site recognition / Integration of provirus / APOBEC3G mediated resistance to HIV-1 infection / heterochromatin / nuclear periphery / exoribonuclease H / exoribonuclease H activity / DNA integration / euchromatin / viral genome integration into host DNA / establishment of integrated proviral latency / RNA-directed DNA polymerase / RNA stem-loop binding / RNA-directed DNA polymerase activity / RNA-DNA hybrid ribonuclease activity / Transferases; Transferring phosphorus-containing groups; Nucleotidyltransferases / viral capsid / response to heat / response to oxidative stress / DNA recombination / DNA-directed DNA polymerase / DNA-binding transcription factor binding / aspartic-type endopeptidase activity / Hydrolases; Acting on ester bonds / DNA-directed DNA polymerase activity / transcription coactivator activity / chromatin remodeling / viral translational frameshifting / chromatin binding / symbiont entry into host cell / positive regulation of transcription by RNA polymerase II / proteolysis / DNA-templated transcription / DNA binding / RNA binding / nucleoplasm / zinc ion binding / nucleus / cytosol
Similarity search - Function
Lens epithelium-derived growth factor, integrase-binding domain / HIV integrase-binding domain superfamily / Lens epithelium-derived growth factor (LEDGF) / dUTPase-like / dUTPase / dUTPase, trimeric / dUTPase-like superfamily / TFIIS/LEDGF domain superfamily / gag protein p24 N-terminal domain / domain with conserved PWWP motif ...Lens epithelium-derived growth factor, integrase-binding domain / HIV integrase-binding domain superfamily / Lens epithelium-derived growth factor (LEDGF) / dUTPase-like / dUTPase / dUTPase, trimeric / dUTPase-like superfamily / TFIIS/LEDGF domain superfamily / gag protein p24 N-terminal domain / domain with conserved PWWP motif / PWWP domain / PWWP domain profile. / PWWP domain / Reverse transcriptase connection / Reverse transcriptase connection domain / Integrase Zinc binding domain / Zinc finger integrase-type profile. / Integrase, C-terminal domain superfamily, retroviral / Integrase, N-terminal zinc-binding domain / Integrase-like, N-terminal / Integrase, C-terminal, retroviral / Integrase DNA binding domain profile. / RNase H / Integrase core domain / Integrase, catalytic core / Integrase catalytic domain profile. / RNase H type-1 domain profile. / Ribonuclease H domain / Retroviral nucleocapsid Gag protein p24, C-terminal domain / Gag protein p24 C-terminal domain / Retropepsins / Retroviral aspartyl protease / Aspartyl protease, retroviral-type family profile. / Peptidase A2A, retrovirus, catalytic / Retrovirus capsid, C-terminal / Reverse transcriptase (RNA-dependent DNA polymerase) / Reverse transcriptase domain / Reverse transcriptase (RT) catalytic domain profile. / Retrovirus capsid, N-terminal / zinc finger / Zinc knuckle / Zinc finger, CCHC-type superfamily / Zinc finger, CCHC-type / Zinc finger CCHC-type profile. / Aspartic peptidase, active site / Eukaryotic and viral aspartyl proteases active site. / Aspartic peptidase domain superfamily / Ribonuclease H superfamily / Ribonuclease H-like superfamily / Reverse transcriptase/Diguanylate cyclase domain / DNA/RNA polymerase superfamily
Similarity search - Domain/homology
PC4 and SFRS1-interacting protein / Gag-Pol polyprotein
Similarity search - Component
Biological speciesVisna-maedi virus / Visna/maedi virus EV1 KV1772 / Homo sapiens (human) / synthetic construct (others)
Methodsingle particle reconstruction / cryo EM / Resolution: 2.8 Å
AuthorsPunch EK / Hope J / Cherepanov P
Funding support United States, United Kingdom, 4 items
OrganizationGrant numberCountry
National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)U54AI170791 United States
Wellcome TrustCC2058 United Kingdom
Medical Research Council (MRC, United Kingdom)CC2058 United Kingdom
Cancer Research UKCC2058 United Kingdom
CitationJournal: To Be Published
Title: Core nucleosomes are refractive for lentiviral integration
Authors: Hope J / Punch EK / Cook NJ / Singer MR / Joshi D / Singh PK / Nans A / Engelman AN / Cherepanov P
History
DepositionJul 21, 2025-
Header (metadata) releaseAug 5, 2026-
Map releaseAug 5, 2026-
UpdateAug 5, 2026-
Current statusAug 5, 2026Processing site: PDBe / Status: Released

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Structure visualization

Supplemental images

emd_54481.png

Downloads & links

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Map

FileDownload / File: emd_54481.map.gz / Format: CCP4 / Size: 325 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
0.95 Å/pix.
x 440 pix.
= 418. Å		0.95 Å/pix.
x 440 pix.
= 418. Å		0.95 Å/pix.
x 440 pix.
= 418. Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 0.95 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.1
Minimum - Maximum-2.470274 - 4.245279
Average (Standard dev.)0.0018172421 (±0.03890359)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions440440440
Spacing440440440
CellA=B=C: 418.0 Å
α=β=γ: 90.0 °

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Supplemental data

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Additional map: #1

Fileemd_54481_additional_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: #2

Fileemd_54481_half_map_1.map
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: #1

Fileemd_54481_half_map_2.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 : MVV STC intasome in complex with LEDGF

EntireName: MVV STC intasome in complex with LEDGF
Components
  • Complex: MVV STC intasome in complex with LEDGF
    • Protein or peptide: Gag-Pol polyprotein
    • Protein or peptide: PC4 and SFRS1-interacting protein
    • DNA: DNA EV392
    • DNA: DNA EV306
    • DNA: DNA EV391
  • Ligand: ZINC ION

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Supramolecule #1: MVV STC intasome in complex with LEDGF

SupramoleculeName: MVV STC intasome in complex with LEDGF / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#5
Details: Integrase and LEDGF were produced in E. coli. The complex was assembled in vitro.
Source (natural)Organism: Visna-maedi virus / Strain: KV1772
Molecular weightTheoretical: 902 KDa

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Macromolecule #1: Gag-Pol polyprotein

MacromoleculeName: Gag-Pol polyprotein / type: protein_or_peptide / ID: 1 / Number of copies: 16 / Enantiomer: LEVO
Source (natural)Organism: Visna/maedi virus EV1 KV1772 / Strain: KV1772
Molecular weightTheoretical: 32.368826 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: WIENIPLAEE EHNKWHQDAV SLHLEFGIPR TAAEDIVQQC DVCQENKMPS TLRGSNKRGI DHWQVDYTHY EDKIILVWVE TNSGLIYAE RVKGETGQEF RVQTMKWYAM FAPKSLQSDN GPAFVAESTQ LLMKYLGIEH TTGIPWNPQS QALVERTHQT L KNTLEKLI ...String:
WIENIPLAEE EHNKWHQDAV SLHLEFGIPR TAAEDIVQQC DVCQENKMPS TLRGSNKRGI DHWQVDYTHY EDKIILVWVE TNSGLIYAE RVKGETGQEF RVQTMKWYAM FAPKSLQSDN GPAFVAESTQ LLMKYLGIEH TTGIPWNPQS QALVERTHQT L KNTLEKLI PMFNAFESAL AGTLITLNIK RKGGLGTSPM DIFIFNKEQQ RIQQQSKSKQ EKIRFCYYRT RKRGHPGEWQ GP TQVLWGG DGAIVVKDRG TDRYLVIANK DVKFIPPPKE IQKE

UniProtKB: Gag-Pol polyprotein

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Macromolecule #2: PC4 and SFRS1-interacting protein

MacromoleculeName: PC4 and SFRS1-interacting protein / type: protein_or_peptide / ID: 2 / Details: LEDGF/p75 protein / Number of copies: 10 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 60.224453 KDa
Recombinant expressionOrganism: Escherichia coli BL21(DE3) (bacteria)
SequenceString: MTRDFKPGDL IFAKMKGYPH WPARVDEVPD GAVKPPTNKL PIFFFGTHET AFLGPKDIFP YSENKEKYGK PNKRKGFNEG LWEIDNNPK VKFSSQQAAT KQSNASSDVE VEEKETSVSK EDTDHEEKAS NEDVTKAVDI TTPKAARRGR KRKAEKQVET E EAGVVTTA ...String:
MTRDFKPGDL IFAKMKGYPH WPARVDEVPD GAVKPPTNKL PIFFFGTHET AFLGPKDIFP YSENKEKYGK PNKRKGFNEG LWEIDNNPK VKFSSQQAAT KQSNASSDVE VEEKETSVSK EDTDHEEKAS NEDVTKAVDI TTPKAARRGR KRKAEKQVET E EAGVVTTA TASVNLKVSP KRGRPAATEV KIPKPRGRPK MVKQPCPSES DIITEEDKSK KKGQEEKQPK KQPKKDEEGQ KE EDKPRKE PDKKEGKKEV ESKRKNLAKT GVTSTSDSEE EGDDQEGEKK RKGGRNFQTA HRRNMLKGQH EKEAADRKRK QEE QMETEQ QNKDEGKKPE VKKVEKKRET SMDSRLQRIH AEIKNSLKID NLDVNRCIEA LDELASLQVT MQQAQKHTEM ITTL KKIRR FKVSQVIMEK STMLYNKFKN MFLVGEGDSV ITQVLNKSLA EQRQHEEANK TKDQGKKGPN KKLEKEQTGS KTLNG GSDA QDGNQPQHNG ESNEDSKDNH EASTKKKPSS EERETEISLK DSTLDN

UniProtKB: PC4 and SFRS1-interacting protein

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Macromolecule #3: DNA EV392

MacromoleculeName: DNA EV392 / type: dna / ID: 3 / Details: synthetic oligonucleotide / Number of copies: 2 / Classification: DNA
Source (natural)Organism: synthetic construct (others)
Molecular weightTheoretical: 9.863336 KDa
SequenceString:
(DC)(DC)(DC)(DG)(DT)(DA)(DT)(DC)(DC)(DG) (DC)(DT)(DT)(DA)(DA)(DG)(DT)(DG)(DA)(DC) (DT)(DT)(DG)(DA)(DT)(DT)(DA)(DG)(DG) (DG)(DT)(DG)

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Macromolecule #4: DNA EV306

MacromoleculeName: DNA EV306 / type: dna / ID: 4 / Details: synthetic oligonucleotide / Number of copies: 2 / Classification: DNA
Source (natural)Organism: synthetic construct (others)
Molecular weightTheoretical: 8.943719 KDa
SequenceString:
(DG)(DC)(DT)(DG)(DC)(DG)(DA)(DG)(DA)(DT) (DC)(DC)(DG)(DC)(DT)(DC)(DC)(DG)(DG)(DT) (DG)(DT)(DT)(DG)(DC)(DA)(DC)(DG)(DG)

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Macromolecule #5: DNA EV391

MacromoleculeName: DNA EV391 / type: dna / ID: 5 / Details: synthetic oligonucleotide / Number of copies: 2 / Classification: DNA
Source (natural)Organism: synthetic construct (others)
Molecular weightTheoretical: 19.990801 KDa
SequenceString: (DC)(DC)(DG)(DT)(DG)(DC)(DA)(DA)(DC)(DA) (DC)(DC)(DG)(DG)(DA)(DG)(DC)(DG)(DG)(DA) (DT)(DC)(DT)(DC)(DG)(DC)(DA)(DG)(DT) (DC)(DG)(DA)(DC)(DC)(DA)(DC)(DC)(DC)(DT) (DA) (DA)(DT)(DC)(DA)(DA)(DG) ...String:
(DC)(DC)(DG)(DT)(DG)(DC)(DA)(DA)(DC)(DA) (DC)(DC)(DG)(DG)(DA)(DG)(DC)(DG)(DG)(DA) (DT)(DC)(DT)(DC)(DG)(DC)(DA)(DG)(DT) (DC)(DG)(DA)(DC)(DC)(DA)(DC)(DC)(DC)(DT) (DA) (DA)(DT)(DC)(DA)(DA)(DG)(DT)(DC) (DA)(DC)(DT)(DT)(DA)(DA)(DG)(DC)(DG)(DG) (DA)(DT) (DA)(DC)(DG)(DG)(DG)

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Macromolecule #6: ZINC ION

MacromoleculeName: ZINC ION / type: ligand / ID: 6 / Number of copies: 14 / Formula: ZN
Molecular weightTheoretical: 65.409 Da

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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

BufferpH: 6.5
Sugar embeddingMaterial: vitreous ice
GridModel: Quantifoil R1.2/1.3 / Material: GOLD / Mesh: 300 / Support film - Material: GRAPHENE OXIDE / Support film - topology: HOLEY / Pretreatment - Type: GLOW DISCHARGE
VitrificationCryogen name: ETHANE / Instrument: FEI VITROBOT MARK IV
Details150 mM NaCl, 20 mM BisTris-HCl pH 6.5, 3 mM CaCl2

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Electron microscopy

MicroscopeTFS KRIOS
Specialist opticsEnergy filter - Name: TFS Selectris / Energy filter - Slit width: 7 eV
Image recordingFilm or detector model: FEI FALCON IV (4k x 4k) / Average electron dose: 40.8 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsC2 aperture diameter: 50.0 µm / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 3.3000000000000003 µm / Nominal defocus min: 1.5 µm / Nominal magnification: 130000
Sample stageCooling holder cryogen: NITROGEN
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

Particle selectionNumber selected: 60999
CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
Startup modelType of model: OTHER
Details: non-uniform refinement from cryosparc from smaller dataset collected on the same grid from Talos 200kV
Final reconstructionResolution.type: BY AUTHOR / Resolution: 2.8 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: cryoSPARC (ver. 4.5.3) / Number images used: 60999
Initial angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: RELION (ver. 4.0.0)
Final angle assignmentType: MAXIMUM LIKELIHOOD / Software - Name: cryoSPARC (ver. 4.5.3)
Final 3D classificationSoftware - Name: cryoSPARC (ver. 4.5.3)
FSC plot (resolution estimation)

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Atomic model buiding 1

Initial model
PDB IDChain

7u32

source_name: PDB, initial_model_type: experimental model

3hph

source_name: PDB, initial_model_type: experimental model
RefinementSpace: REAL / Protocol: RIGID BODY FIT
Output model

PDB-9s28:
MVV STC intasome in complex with LEDGF

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