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Open data
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Basic information
| Entry | ![]()  | |||||||||
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| Title | FAdV-C4 Aviadenovirus structure, strain KR5 | |||||||||
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 Sample | 
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 Keywords | adenovirus / fowl / highly thermostable / VIRUS | |||||||||
| Function / homology |  Function and homology informationhexon binding / viral capsid, decoration / T=25 icosahedral viral capsid / microtubule-dependent intracellular transport of viral material towards nucleus / viral capsid / host cell / endocytosis involved in viral entry into host cell / symbiont entry into host cell / virion attachment to host cell / host cell nucleus / structural molecule activity Similarity search - Function  | |||||||||
| Biological species |  Fowl aviadenovirus C | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 3.4 Å | |||||||||
 Authors | Perez-Illana MP / Schachnner A / Condezo GN / Hernando-Perez M / Martinez M / Marabini R / Hess M / San Martin C | |||||||||
| Funding support | 2 items 
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 Citation |  Journal: PLoS Pathog / Year: 2025Title: Aviadenovirus structure: A highly thermostable capsid in the absence of stabilizing proteins. Authors: Marta Pérez-Illana / Anna Schachner / Mercedes Hernando-Pérez / Gabriela N Condezo / Alberto Paradela / Marta Martínez / Roberto Marabini / Michael Hess / Carmen San Martín /   ![]() Abstract: High-resolution structural studies have mainly focused on two out of the six adenovirus genera: mastadenoviruses and atadenoviruses. Here we report the high-resolution structure of an aviadenovirus, ...High-resolution structural studies have mainly focused on two out of the six adenovirus genera: mastadenoviruses and atadenoviruses. Here we report the high-resolution structure of an aviadenovirus, the poultry pathogen fowl adenovirus serotype 4 (FAdV-C4). FAdV-C4 virions are highly thermostable, despite lacking minor coat and core proteins shown to stabilize the mast- and atadenovirus particles, having no genus-specific cementing proteins, and packaging a 25% longer genome. Unique structural features of the FAdV-C4 hexon include a large insertion at the trimer equatorial region, and a long N-terminal tail. Protein IIIa conformation is closer to atadenoviruses than to mastadenoviruses, while protein VIII diverges from all previously reported structures. We interpret these differences in light of adenovirus evolution. Finally, we discuss the possible role of core composition in determining capsid stability properties. These results enlarge our view on the structural diversity of adenoviruses, and provide useful information to counteract fowl pathogens or use non-human adenoviruses as vectors.  | |||||||||
| History | 
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Structure visualization
| Supplemental images | 
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Downloads & links
-EMDB archive
| Map data |  emd_19401.map.gz | 1.5 GB |  EMDB map data format | |
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| Header (meta data) |  emd-19401-v30.xml emd-19401.xml | 22.7 KB 22.7 KB  | Display Display  |  EMDB header | 
| FSC (resolution estimation) |  emd_19401_fsc.xml | 22.1 KB | Display |  FSC data file | 
| Images |  emd_19401.png | 274.7 KB | ||
| Filedesc metadata |  emd-19401.cif.gz | 7.3 KB | ||
| Others |  emd_19401_half_map_1.map.gz emd_19401_half_map_2.map.gz | 1.3 GB 1.3 GB  | ||
| Archive directory |  http://ftp.pdbj.org/pub/emdb/structures/EMD-19401 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-19401 | HTTPS FTP  | 
-Validation report
| Summary document |  emd_19401_validation.pdf.gz | 1.2 MB | Display |  EMDB validaton report | 
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| Full document |  emd_19401_full_validation.pdf.gz | 1.2 MB | Display | |
| Data in XML |  emd_19401_validation.xml.gz | 33.9 KB | Display | |
| Data in CIF |  emd_19401_validation.cif.gz | 46.8 KB | Display | |
| Arichive directory |  https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-19401 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-19401 | HTTPS FTP  | 
-Related structure data
| Related structure data | ![]() 8roqMC M: atomic model generated by this map C: citing same article (  | 
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| Similar structure data | Similarity search - Function & homology  F&H Search | 
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Links
| EMDB pages |  EMDB (EBI/PDBe) /  EMDataResource | 
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| Related items in Molecule of the Month | 
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Map
| File |  Download / File: emd_19401.map.gz / Format: CCP4 / Size: 1.6 GB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES) | ||||||||||||||||||||||||||||||||||||
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| Projections & slices | Image control
 
 Images are generated by Spider.  | ||||||||||||||||||||||||||||||||||||
| Voxel size | X=Y=Z: 1.375 Å | ||||||||||||||||||||||||||||||||||||
| Density | 
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML: 
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-Supplemental data
-Half map: #2
| File | emd_19401_half_map_1.map | ||||||||||||
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| Projections & Slices | 
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| Density Histograms | 
-Half map: #1
| File | emd_19401_half_map_2.map | ||||||||||||
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| Projections & Slices | 
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| Density Histograms | 
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Sample components
-Entire : Fowl aviadenovirus C
| Entire | Name:  Fowl aviadenovirus C | 
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| Components | 
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-Supramolecule #1: Fowl aviadenovirus C
| Supramolecule | Name: Fowl aviadenovirus C / type: virus / ID: 1 / Parent: 0 / Macromolecule list: all / NCBI-ID: 190063 / Sci species name: Fowl aviadenovirus C / Sci species strain: KR5 / Virus type: VIRUS-LIKE PARTICLE / Virus isolate: SPECIES / Virus enveloped: No / Virus empty: No | 
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| Host (natural) | Organism: ![]()  | 
-Macromolecule #1: Hexon protein
| Macromolecule | Name: Hexon protein / type: protein_or_peptide / ID: 1 / Number of copies: 12 / Enantiomer: LEVO | 
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| Source (natural) | Organism:  Fowl aviadenovirus C | 
| Molecular weight | Theoretical: 106.129789 KDa | 
| Sequence | String: MAALTPDLTT ATPRLQYFHI AGPGTREYLS EDLQQFISAT GSYFDLKNKF RQTVVAPTRN VTTEKAQRLQ IRFYPIQTDD  TSTGYRVRY NINVGDGWVL DMGSTYFDIK GILDRGPSFK PYCGTAYNPL APKESMFNNW SETAPGQNVS ASGQLSNVYT N TSTTKDTT  ...String:  MAALTPDLTT ATPRLQYFHI AGPGTREYLS EDLQQFISAT GSYFDLKNKF RQTVVAPTRN VTTEKAQRLQ IRFYPIQTDD  TSTGYRVRY NINVGDGWVL DMGSTYFDIK GILDRGPSFK PYCGTAYNPL APKESMFNNW SETAPGQNVS ASGQLSNVYT N TSTTKDTT AAQVTKISGV FPNPNQGPGI NPLRQVENAN TGVLGRFAKS QYNYAYGAYV KPVAADGSQS LTQTPYWIMN NA GTEYLGA VAVEDYTNSL SYPDTMIVPP PEDYDDYNIG TTRALRPNYI GFRDNFINLL YHDSGVCSGT LNSERSGMNV VVE LPDRNT ELSYQYMLAD MMSRHHYFAL WNQAVDQYDP EVRVFSNDGY EEGAPSYAFN PEAVGAGEGY GPDLSQIKLY TNNT AANDK NTAVTNATTN FYFGTVPSYE IDISATQRRN FIMANIAEYL PDRYKFSISG FDATSVAPTT YEYMNKRVPL TNVVD MFTN VGARWSIDQM DNVNPFNHHR NWGLKYRSQL LGNSRYVNFH IQVPQKFFAI KNLLLLSGSY TYEWVLRKDP NMILQS SLG NDLRADGASI IYNEVNLMAN FMPMDHNTSN QLELMLRNAT NDQTFVDYLG AKNALYSVPA GSTALTINIP ARTWEGM RG WSFTRIKAAE TPQLGAQYDV NFKYSGSIAY SDGGFYLSHT FRNMSILFDT SINWPGNDRL LTPNMFEIKR SVALDTEG F TMSQCDITKD WYLIQMATNY NFVYNGYRFW PDRQYFHYDF LRNFDPMTRQ GPNFALPGLF DLVSYTPTTD NSGEQPSQE  AVRNNSGFIA PRSWPVWSAH QGESWPANWP YPLCGQQAIQ PGQVLSYKKF LCDNYLWTIP FSSDFMYMGE LTDLGQNPMY  TNNSHSMVI NFELDPMDDP TYVYMLYGVF DTVRVNQPER NVLAMAYFRT PFATGNAV UniProtKB: Hexon protein  | 
-Macromolecule #2: Penton protein
| Macromolecule | Name: Penton protein / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO | 
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| Source (natural) | Organism:  Fowl aviadenovirus C | 
| Molecular weight | Theoretical: 57.448238 KDa | 
| Sequence | String: MWGLQPPTSI PPPPPPTELT PSTYPAMVNG YPPPAASAQS CSSSGGQSEL YMPLQRVMAP TGGRNSIKYR DYTPCRNTTK  LFYVDNKAS DIDTYNKDAN HSNFRTTVIH NQDLDADTAA TESIQLDNRS CWGGDLKTAV RTNCPNVSSF FQSNSVRVRM M WKRDPPTS  ...String:  MWGLQPPTSI PPPPPPTELT PSTYPAMVNG YPPPAASAQS CSSSGGQSEL YMPLQRVMAP TGGRNSIKYR DYTPCRNTTK  LFYVDNKAS DIDTYNKDAN HSNFRTTVIH NQDLDADTAA TESIQLDNRS CWGGDLKTAV RTNCPNVSSF FQSNSVRVRM M WKRDPPTS TAPPSAVGSG YSVPGAQYKW YDLTVPEGNY ALCELIDLLN EGIVQLYLSE GRQNNVQKSD IGVKFDTRNF GL LRDPVTG LVTPGTYVYK GYHPDIVLLP GCAIDFTYSR LSLLLGIGKR EPYSKGFVIT YEDLQGGDIP ALLDLDSVDV NDA DGEVIE LDNAAPLLHD SAGVSYNVIY DQVTGKPVTA YRSWMLAYNV PNSQANQTTL LTVPDMAGGI GAMYTSLPDT FIAP TGFKE DNTTNLCPVV GMNLFPTYNK IYYQAASTYV QRLENSCQSA TAAFNRFPEN EILKQAPPMN VSSVCDNQPA VVQQG VLPV KSSLPGLQRV LITDDQRRPI PYVYKSIATV QPTVLSSATL Q UniProtKB: Penton protein  | 
-Macromolecule #3: PIIIa
| Macromolecule | Name: PIIIa / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO | 
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| Source (natural) | Organism:  Fowl aviadenovirus C | 
| Molecular weight | Theoretical: 65.326297 KDa | 
| Sequence | String: MSSTEVFGAL APVGRTEVAD ALSSHANSKD ARSLRYEPYA NRLIKLQTAM VPPKVDGTSE RVAEVVKGLA EQGAIYPDQM  GAIHSDLLN RVYTWNSMGV QESIQALVND VIHGQNKVLQ DELARTREIA NASMLTRFFD SLYKTVDRGQ RNFEGFKKLL R LFVNNVPN  ...String:  MSSTEVFGAL APVGRTEVAD ALSSHANSKD ARSLRYEPYA NRLIKLQTAM VPPKVDGTSE RVAEVVKGLA EQGAIYPDQM  GAIHSDLLN RVYTWNSMGV QESIQALVND VIHGQNKVLQ DELARTREIA NASMLTRFFD SLYKTVDRGQ RNFEGFKKLL R LFVNNVPN AEVYSSGGSF SLQINMGGQS QNINLTNAFD NLKDIWGARW DAVNNPRIGA LLTPNTRALL FFVSTFYDYG SM EPGSYLD NLMRLYKEAI RADTDAEGDA IMELGDAGAN LNLKFNQYKD TLNYLLQNKP SVPQTGPLEM SPEQESLFKY LMR QLRRAL KDGVNSDIAI STMAQYVDPR LYTSNKVFID KLQNYLLMAS ARNPYYYKTI VLDPHWVPPA GLYTDNFVIP EMMP NFSDF ASELEYGGPS RDEYFDDSPF RPPPQKKFTE KEQADYDSLI NFFDSTLGVQ SEAGWIADHR LPQAFDGALN VSERT PYNT PLPDDAPMRS RNASVSSATD ALGQLKLSGT GGAGFFDSLK PSVGTRRSTG LAKGLAGTGQ PPCPWPASVG YASAGY GPA RGIRGSGLAR RALAARGLRQ GKRLRFY UniProtKB: PIIIa  | 
-Macromolecule #4: Pre-hexon-linking protein VIII
| Macromolecule | Name: Pre-hexon-linking protein VIII / type: protein_or_peptide / ID: 4 / Number of copies: 2 / Enantiomer: LEVO | 
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| Source (natural) | Organism:  Fowl aviadenovirus C | 
| Molecular weight | Theoretical: 26.882158 KDa | 
| Sequence | String: MNLLNAAPTP YVWKYNPVTG KCAGAQQNYG ATIDWVLPGG NSFAYAADEI RRRFPEPAVT RAITARFEAE SDQQPYAGPH  ETNIITADV VRSGPPPSAV YPFDPSGVQR VQLSGGMMGG RTEGRMQLSG GLTEGRMQLA GGAAGKLPTR ARPTLRPPRW C GTTLTGNG  ...String:  MNLLNAAPTP YVWKYNPVTG KCAGAQQNYG ATIDWVLPGG NSFAYAADEI RRRFPEPAVT RAITARFEAE SDQQPYAGPH  ETNIITADV VRSGPPPSAV YPFDPSGVQR VQLSGGMMGG RTEGRMQLSG GLTEGRMQLA GGAAGKLPTR ARPTLRPPRW C GTTLTGNG LPADYPEMTP DAFKYYLRVQ GPSQEVDEPG VMSQRQFMTT FLPAMVPHPF DSESPDAFPA YFSSVYKGTN AF EPVFWQG UniProtKB: Pre-hexon-linking protein VIII  | 
-Experimental details
-Structure determination
| Method | cryo EM | 
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 Processing | single particle reconstruction | 
| Aggregation state | particle | 
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Sample preparation
| Buffer | pH: 7.8 | 
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| Vitrification | Cryogen name: ETHANE | 
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Electron microscopy
| Microscope | FEI TITAN KRIOS | 
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| Image recording | Film or detector model: FEI FALCON III (4k x 4k) / Average electron dose: 40.5 e/Å2 | 
| Electron beam | Acceleration voltage: 300 kV / Electron source:  FIELD EMISSION GUN | 
| Electron optics | Calibrated magnification: 95890 / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.5 µm / Nominal defocus min: 1.0 µm | 
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company  | 
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Fowl aviadenovirus C
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FIELD EMISSION GUN

