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- EMDB-77024: Cryo-EM structure of HAdV-C6 hexon trimer in complex with prothro... -

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Entry
Database: EMDB / ID: EMD-77024
TitleCryo-EM structure of HAdV-C6 hexon trimer in complex with prothrombin (FII)
Map dataHAdV-C6 hexon trimer in complex with human coagulation factor FII
Sample
  • Complex: Purified Human adenovirus type 6 hexon trimer in complex with prothrombin (FII)
    • Protein or peptide: Hexon protein
    • Protein or peptide: Prothrombin
  • Ligand: CALCIUM ION
Keywordsadenovirus / hexon / coagulation factor II / virus-host interaction / cryo-EM / virus capsid / VIRAL PROTEIN
Function / homology
Function and homology information


T=25 icosahedral viral capsid / microtubule-dependent intracellular transport of viral material towards nucleus / : / thrombospondin receptor activity / thrombin / thrombin-activated receptor signaling pathway / Defective factor XII causes hereditary angioedema / negative regulation of astrocyte differentiation / regulation of blood coagulation / neutrophil-mediated killing of gram-negative bacterium ...T=25 icosahedral viral capsid / microtubule-dependent intracellular transport of viral material towards nucleus / : / thrombospondin receptor activity / thrombin / thrombin-activated receptor signaling pathway / Defective factor XII causes hereditary angioedema / negative regulation of astrocyte differentiation / regulation of blood coagulation / neutrophil-mediated killing of gram-negative bacterium / positive regulation of phospholipase C-activating G protein-coupled receptor signaling pathway / Defective F8 cleavage by thrombin / ligand-gated ion channel signaling pathway / Platelet Aggregation (Plug Formation) / positive regulation of collagen biosynthetic process / negative regulation of platelet activation / negative regulation of blood coagulation / negative regulation of fibrinolysis / blood coagulation, fibrin clot formation / positive regulation of blood coagulation / Transport of gamma-carboxylated protein precursors from the endoplasmic reticulum to the Golgi apparatus / : / Gamma-carboxylation of protein precursors / Removal of aminoterminal propeptides from gamma-carboxylated proteins / regulation of cytosolic calcium ion concentration / fibrinolysis / : / negative regulation of proteolysis / negative regulation of cytokine production involved in inflammatory response / Regulation of Complement cascade / acute-phase response / Cell surface interactions at the vascular wall / positive regulation of release of sequestered calcium ion into cytosol / Peptide ligand-binding receptors / growth factor activity / positive regulation of receptor signaling pathway via JAK-STAT / lipopolysaccharide binding / platelet activation / response to wounding / positive regulation of protein localization to nucleus / Golgi lumen / Regulation of Insulin-like Growth Factor (IGF) transport and uptake by Insulin-like Growth Factor Binding Proteins (IGFBPs) / positive regulation of reactive oxygen species metabolic process / blood coagulation / positive regulation of insulin secretion / regulation of cell shape / antimicrobial humoral immune response mediated by antimicrobial peptide / host cell / heparin binding / Thrombin signalling through proteinase activated receptors (PARs) / positive regulation of cell growth / blood microparticle / G alpha (q) signalling events / cell surface receptor signaling pathway / positive regulation of phosphatidylinositol 3-kinase/protein kinase B signal transduction / endoplasmic reticulum lumen / receptor ligand activity / signaling receptor binding / serine-type endopeptidase activity / calcium ion binding / positive regulation of cell population proliferation / symbiont entry into host cell / host cell nucleus / structural molecule activity / proteolysis / : / extracellular exosome / extracellular region / plasma membrane
Similarity search - Function
Adenovirus hexon protein / Adenovirus Pll, hexon, N-terminal / Adenovirus Pll, hexon, C-terminal / Adenovirus Pll, hexon, subdomain 2 / Hexon, adenovirus major coat protein, N-terminal domain / Hexon, adenovirus major coat protein, C-terminal domain / Group II dsDNA virus coat/capsid protein / Prothrombin/thrombin / Thrombin light chain / Thrombin light chain domain superfamily ...Adenovirus hexon protein / Adenovirus Pll, hexon, N-terminal / Adenovirus Pll, hexon, C-terminal / Adenovirus Pll, hexon, subdomain 2 / Hexon, adenovirus major coat protein, N-terminal domain / Hexon, adenovirus major coat protein, C-terminal domain / Group II dsDNA virus coat/capsid protein / Prothrombin/thrombin / Thrombin light chain / Thrombin light chain domain superfamily / : / Thrombin light chain / Kringle domain / Kringle / Kringle, conserved site / Kringle superfamily / Kringle domain signature. / Kringle domain profile. / Kringle domain / Vitamin K-dependent carboxylation/gamma-carboxyglutamic (GLA) domain / Gamma-carboxyglutamic acid-rich (GLA) domain / Gamma-carboxyglutamic acid-rich (GLA) domain superfamily / Vitamin K-dependent carboxylation domain. / Gla domain profile. / Domain containing Gla (gamma-carboxyglutamate) residues. / Kringle-like fold / Serine proteases, trypsin family, histidine active site / Serine proteases, trypsin family, serine active site / Serine proteases, trypsin family, histidine active site. / Serine proteases, trypsin family, serine active site. / Peptidase S1A, chymotrypsin family / Serine proteases, trypsin domain profile. / Trypsin-like serine protease / Serine proteases, trypsin domain / Trypsin / Peptidase S1, PA clan, chymotrypsin-like fold / Peptidase S1, PA clan
Similarity search - Domain/homology
Hexon protein / Prothrombin
Similarity search - Component
Biological speciesHuman adenovirus 6 / Homo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.22 Å
AuthorsMa OX / Reddy VS
Funding support United States, 1 items
OrganizationGrant numberCountry
National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)AI161367 United States
CitationJournal: To Be Published
Title: Structural requirements of blood factors binding to soluble hexon trimers with implications for adenovirus cell targeting and immune evasion
Authors: Ma OX / Reddy VS
History
DepositionMay 3, 2026-
Header (metadata) releaseJul 8, 2026-
Map releaseJul 8, 2026-
UpdateJul 8, 2026-
Current statusJul 8, 2026Processing site: RCSB / Status: Released

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Structure visualization

Supplemental images

emd_77024.png

Downloads & links

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Map

FileReleased
AnnotationHAdV-C6 hexon trimer in complex with human coagulation factor FII
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
0.85 Å/pix.
x 256 pix.
= 217.6 Å		0.85 Å/pix.
x 256 pix.
= 217.6 Å		0.85 Å/pix.
x 256 pix.
= 217.6 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 0.85 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.05
Minimum - Maximum-0.024404274 - 1.7517995
Average (Standard dev.)0.0051913173 (±0.047555916)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin-128-128-128
Dimensions256256256
Spacing256256256
CellA=B=C: 217.6 Å
α=β=γ: 90.0 °

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Supplemental data

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Half map: half map of HAdV-C6 hexon trimer in complex...

Fileemd_77024_half_map_1.map
Annotationhalf map of HAdV-C6 hexon trimer in complex with human coagulation factor FII
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: half map of HAdV-C6 hexon trimer in complex...

Fileemd_77024_half_map_2.map
Annotationhalf map of HAdV-C6 hexon trimer in complex with human coagulation factor FII
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Sample components

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Entire : Purified Human adenovirus type 6 hexon trimer in complex with pro...

EntireName: Purified Human adenovirus type 6 hexon trimer in complex with prothrombin (FII)
Components
  • Complex: Purified Human adenovirus type 6 hexon trimer in complex with prothrombin (FII)
    • Protein or peptide: Hexon protein
    • Protein or peptide: Prothrombin
  • Ligand: CALCIUM ION

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Supramolecule #1: Purified Human adenovirus type 6 hexon trimer in complex with pro...

SupramoleculeName: Purified Human adenovirus type 6 hexon trimer in complex with prothrombin (FII)
type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#2
Source (natural)Organism: Human adenovirus 6
Molecular weightTheoretical: 400 KDa

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Macromolecule #1: Hexon protein

MacromoleculeName: Hexon protein / type: protein_or_peptide / ID: 1
Details: The modeled structure lacks the N-terminal residues 1-6, an internal region corresponding to residues 139-164, and a short segment around residues 445-452, as well as the C-terminal residues ...Details: The modeled structure lacks the N-terminal residues 1-6, an internal region corresponding to residues 139-164, and a short segment around residues 445-452, as well as the C-terminal residues 948-952. These regions were not included in the model due to the absence of well-defined cryo-EM density.
Number of copies: 3 / Enantiomer: LEVO
Source (natural)Organism: Human adenovirus 6
Molecular weightTheoretical: 108.635133 KDa
SequenceString: MATPSMMPQW SYMHISGQDA SEYLSPGLVQ FARATETYFS LNNKFRNPTV APTHDVTTDR SQRLTLRFIP VDREDTAYSY KARFTLAVG DNRVLDMAST YFDIRGVLDR GPTFKPYSGT AYNALAPKGA PNSCEWEQNE TAQVDAQELD EEENEANEAQ A REQEQAKK ...String:
MATPSMMPQW SYMHISGQDA SEYLSPGLVQ FARATETYFS LNNKFRNPTV APTHDVTTDR SQRLTLRFIP VDREDTAYSY KARFTLAVG DNRVLDMAST YFDIRGVLDR GPTFKPYSGT AYNALAPKGA PNSCEWEQNE TAQVDAQELD EEENEANEAQ A REQEQAKK THVYAQAPLS GIKITKEGLQ IGTADATVAG AGKEIFADKT FQPEPQVGES QWNEADATAA GGRVLKKTTP MK PCYGSYA RPTNSNGGQG VMVEQNGKLE SQVEMQFFST STNATNEVNN IQPTVVLYSE DVNMETPDTH LSYKPKMGDK NAK VMLGQQ AMPNRPNYIA FRDNFIGLMY YNSTGNMGVL AGQASQLNAV VDLQDRNTEL SYQLLLDSIG DRTRYFSMWN QAVD SYDPD VRIIENHGTE DELPNYCFPL GGIGITDTFQ AVKTTAANGD QGNTTWQKDS TFAERNEIGV GNNFAMEINL NANLW RNFL YSNIALYLPD KLKYNPTNVE ISDNPNTYDY MNKRVVAPGL VDCYINLGAR WSLEYMDNVN PFNHHRNAGL RYRSML LGN GRYVPFHIQV PQKFFAIKNL LLLPGSYTYE WNFRKDVNMV LQSSLGNDLR VDGASIKFDS ICLYATFFPM AHNTAST LE AMLRNDTNDQ SFNDYLSAAN MLYPIPANAT NVPISIPSRN WAAFRGWAFT RLKTKETPSL GSGYDPYYTY SGSIPYLD G TFYLNHTFKK VAITFDSSVS WPGNDRLLTP NEFEIKRSVD GEGYNVAQCN MTKDWFLVQM LANYNIGYQG FYIPESYKD RMYSFFRNFQ PMSRQVVDDT KYKDYQQVGI IHQHNNSGFV GYLAPTMREG QAYPANVPYP LIGKTAVDSI TQKKFLCDRT LWRIPFSSN FMSMGALTDL GQNLLYANSA HALDMTFEVD PMDEPTLLYV LFEVFDVVRV HQPHRGVIET VYLRTPFSAG N ATT

UniProtKB: Hexon protein

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Macromolecule #2: Prothrombin

MacromoleculeName: Prothrombin / type: protein_or_peptide / ID: 2
Details: The modeled prothrombin (FII) corresponds to the N-terminal Gla domain, whereas the signal peptide, propeptide, and the remaining domains (including the kringle domains and serine protease ...Details: The modeled prothrombin (FII) corresponds to the N-terminal Gla domain, whereas the signal peptide, propeptide, and the remaining domains (including the kringle domains and serine protease domain) are not included due to lack of interpretable cryo-EM density. The modeled region contains gamma-carboxyglutamic acid (Gla) residues involved in calcium coordination.
Number of copies: 1 / Enantiomer: LEVO / EC number: thrombin
Source (natural)Organism: Homo sapiens (human) / Tissue: blood
Molecular weightTheoretical: 70.56293 KDa
SequenceString: MAHVRGLQLP GCLALAALCS LVHSQHVFLA PQQARSLLQR VRRANTFL(CGU)(CGU) VRKGNL(CGU)R(CGU)C V (CGU)(CGU)TCSY(CGU)(CGU) AF(CGU)AL(CGU)SSTA TDVFWAKYTA CETARTPRDK LAACLEGNCA EGLGTNYR G HVNITRSGIE ...String:
MAHVRGLQLP GCLALAALCS LVHSQHVFLA PQQARSLLQR VRRANTFL(CGU)(CGU) VRKGNL(CGU)R(CGU)C V (CGU)(CGU)TCSY(CGU)(CGU) AF(CGU)AL(CGU)SSTA TDVFWAKYTA CETARTPRDK LAACLEGNCA EGLGTNYR G HVNITRSGIE CQLWRSRYPH KPEINSTTHP GADLQENFCR NPDSSTTGPW CYTTDPTVRR QECSIPVCGQ DQVTVAMTP RSEGSSVNLS PPLEQCVPDR GQQYQGRLAV TTHGLPCLAW ASAQAKALSK HQDFNSAVQL VENFCRNPDG DEEGVWCYVA GKPGDFGYC DLNYCEEAVE EETGDGLDED SDRAIEGRTA TSEYQTFFNP RTFGSGEADC GLRPLFEKKS LEDKTERELL E SYIDGRIV EGSDAEIGMS PWQVMLFRKS PQELLCGASL ISDRWVLTAA HCLLYPPWDK NFTENDLLVR IGKHSRTRYE RN IEKISML EKIYIHPRYN WRENLDRDIA LMKLKKPVAF SDYIHPVCLP DRETAASLLQ AGYKGRVTGW GNLKETWTAN VGK GQPSVL QVVNLPIVER PVCKDSTRIR ITDNMFCAGY KPDEGKRGDA CEGDSGGPFV MKSPFNNRWY QMGIVSWGEG CDRD GKYGF YTHVFRLKKW IQKVIDQFGE

UniProtKB: Prothrombin

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Macromolecule #3: CALCIUM ION

MacromoleculeName: CALCIUM ION / type: ligand / ID: 3 / Number of copies: 7 / Formula: CA
Molecular weightTheoretical: 40.078 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: 7.2
GridModel: Quantifoil R1.2/1.3 / Material: COPPER / Mesh: 300 / Support film - Material: CARBON / Support film - topology: HOLEY / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Time: 60 sec. / Pretreatment - Pressure: 0.038 kPa
VitrificationCryogen name: ETHANE / Chamber humidity: 98 % / Chamber temperature: 277 K / Instrument: FEI VITROBOT MARK IV

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Electron microscopy

MicroscopeTFS KRIOS
Specialist opticsEnergy filter - Slit width: 20 eV
Image recordingFilm or detector model: GATAN K3 BIOCONTINUUM (6k x 4k) / Number real images: 7275 / Average electron dose: 51.0 e/Å2
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 2.4 µm / Nominal defocus min: 0.8 µm
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

Particle selectionNumber selected: 1099039
CTF correctionType: PHASE FLIPPING ONLY
Startup modelType of model: OTHER / Details: hexon trimer density map from previous study
Final reconstructionResolution.type: BY AUTHOR / Resolution: 3.22 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: cryoSPARC / Number images used: 91729
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD
FSC plot (resolution estimation)

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Atomic model buiding 1

SoftwareName: Coot
RefinementProtocol: FLEXIBLE FIT
Output model

PDB-13er:
Cryo-EM structure of HAdV-C6 hexon trimer in complex with prothrombin (FII)

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