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Yorodumi- EMDB-15930: Structure of Echovirus 11 complexed with DAF (CD55) calculated fr... -
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Basic information
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| Title | Structure of Echovirus 11 complexed with DAF (CD55) calculated from symmetry expansion | |||||||||
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Keywords | Echovirus / receptor / CD55 / DAF / VIRUS | |||||||||
| Function / homology | Function and homology informationregulation of lipopolysaccharide-mediated signaling pathway / negative regulation of complement activation / regulation of complement-dependent cytotoxicity / regulation of complement activation / respiratory burst / positive regulation of CD4-positive, alpha-beta T cell activation / positive regulation of CD4-positive, alpha-beta T cell proliferation / Class B/2 (Secretin family receptors) / symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of RIG-I activity / ficolin-1-rich granule membrane ...regulation of lipopolysaccharide-mediated signaling pathway / negative regulation of complement activation / regulation of complement-dependent cytotoxicity / regulation of complement activation / respiratory burst / positive regulation of CD4-positive, alpha-beta T cell activation / positive regulation of CD4-positive, alpha-beta T cell proliferation / Class B/2 (Secretin family receptors) / symbiont-mediated suppression of host cytoplasmic pattern recognition receptor signaling pathway via inhibition of RIG-I activity / ficolin-1-rich granule membrane / complement activation, classical pathway / transport vesicle / side of membrane / COPI-mediated anterograde transport / endoplasmic reticulum-Golgi intermediate compartment membrane / ribonucleoside triphosphate phosphatase activity / secretory granule membrane / Regulation of Complement cascade / picornain 2A / symbiont-mediated suppression of host mRNA export from nucleus / symbiont genome entry into host cell via pore formation in plasma membrane / picornain 3C / T=pseudo3 icosahedral viral capsid / positive regulation of T cell cytokine production / host cell cytoplasmic vesicle membrane / nucleoside-triphosphate phosphatase / channel activity / positive regulation of cytosolic calcium ion concentration / virus receptor activity / monoatomic ion transmembrane transport / DNA replication / RNA helicase activity / membrane raft / endocytosis involved in viral entry into host cell / Golgi membrane / symbiont-mediated activation of host autophagy / innate immune response / RNA-directed RNA polymerase / cysteine-type endopeptidase activity / viral RNA genome replication / RNA-directed RNA polymerase activity / DNA-templated transcription / lipid binding / Neutrophil degranulation / virion attachment to host cell / host cell nucleus / structural molecule activity / cell surface / proteolysis / RNA binding / extracellular exosome / extracellular region / zinc ion binding / ATP binding / membrane / plasma membrane Similarity search - Function | |||||||||
| Biological species | ![]() Echovirus E11 / Homo sapiens (human) | |||||||||
| Method | single particle reconstruction / cryo EM / Resolution: 3.93 Å | |||||||||
Authors | Stuart DI / Ren J / Qin L / Zhou D | |||||||||
| Funding support | United Kingdom, 1 items
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Citation | Journal: Viruses / Year: 2022Title: Switching of Receptor Binding Poses between Closely Related Enteroviruses. Authors: Daming Zhou / Ling Qin / Helen M E Duyvesteyn / Yuguang Zhao / Tzou-Yien Lin / Elizabeth E Fry / Jingshan Ren / Kuan-Ying A Huang / David I Stuart / ![]() Abstract: Echoviruses, for which there are currently no approved vaccines or drugs, are responsible for a range of human diseases, for example echovirus 11 (E11) is a major cause of serious neonatal morbidity ...Echoviruses, for which there are currently no approved vaccines or drugs, are responsible for a range of human diseases, for example echovirus 11 (E11) is a major cause of serious neonatal morbidity and mortality. Decay-accelerating factor (DAF, also known as CD55) is an attachment receptor for E11. Here, we report the structure of the complex of E11 and the full-length ectodomain of DAF (short consensus repeats, SCRs, 1-4) at 3.1 Å determined by cryo-electron microscopy (cryo-EM). SCRs 3 and 4 of DAF interact with E11 at the southern rim of the canyon via the VP2 EF and VP3 BC loops. We also observe an unexpected interaction between the N-linked glycan (residue 95 of DAF) and the VP2 BC loop of E11. DAF is a receptor for at least 20 enteroviruses and we classify its binding patterns from reported DAF/virus complexes into two distinct positions and orientations, named as E6 and E11 poses. Whilst 60 DAF molecules can attach to the virion in the E6 pose, no more than 30 can attach to E11 due to steric restrictions. Analysis of the distinct modes of interaction and structure and sequence-based phylogenies suggests that the two modes evolved independently, with the E6 mode likely found earlier. | |||||||||
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Structure visualization
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Downloads & links
-EMDB archive
| Map data | emd_15930.map.gz | 125.4 MB | EMDB map data format | |
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| Header (meta data) | emd-15930-v30.xml emd-15930.xml | 17.4 KB 17.4 KB | Display Display | EMDB header |
| Images | emd_15930.png | 76.6 KB | ||
| Filedesc metadata | emd-15930.cif.gz | 6.1 KB | ||
| Others | emd_15930_half_map_1.map.gz emd_15930_half_map_2.map.gz | 226.3 MB 226.3 MB | ||
| Archive directory | http://ftp.pdbj.org/pub/emdb/structures/EMD-15930 ftp://ftp.pdbj.org/pub/emdb/structures/EMD-15930 | HTTPS FTP |
-Validation report
| Summary document | emd_15930_validation.pdf.gz | 1 MB | Display | EMDB validaton report |
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| Full document | emd_15930_full_validation.pdf.gz | 1 MB | Display | |
| Data in XML | emd_15930_validation.xml.gz | 15.5 KB | Display | |
| Data in CIF | emd_15930_validation.cif.gz | 18.4 KB | Display | |
| Arichive directory | https://ftp.pdbj.org/pub/emdb/validation_reports/EMD-15930 ftp://ftp.pdbj.org/pub/emdb/validation_reports/EMD-15930 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 8b9fMC ![]() 8b8rC 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_15930.map.gz / Format: CCP4 / Size: 244.1 MB / 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: 1.05 Å | ||||||||||||||||||||||||||||||||||||
| Density |
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| Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||
| Details | EMDB XML:
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-Supplemental data
-Half map: #2
| File | emd_15930_half_map_1.map | ||||||||||||
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| Density Histograms |
-Half map: #1
| File | emd_15930_half_map_2.map | ||||||||||||
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Sample components
-Entire : Complex of Echovirus 11 with DAF
| Entire | Name: Complex of Echovirus 11 with DAF |
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| Components |
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-Supramolecule #1: Complex of Echovirus 11 with DAF
| Supramolecule | Name: Complex of Echovirus 11 with DAF / type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#4 |
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| Source (natural) | Organism: ![]() Echovirus E11 |
-Macromolecule #1: Complement decay-accelerating factor
| Macromolecule | Name: Complement decay-accelerating factor / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO |
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| Source (natural) | Organism: Homo sapiens (human) |
| Molecular weight | Theoretical: 29.771059 KDa |
| Recombinant expression | Organism: Homo sapiens (human) |
| Sequence | String: (MSE)GCVAETGDC GLPPDVPNAQ PALEGRTSFP EDTVITYKCE ESFVKIPGEK DSVICLKGSQ WSDIEEFCNR SCEVPT RLN SASLKQPYIT QNYFPVGTVV EYECRPGYRR EPSLSPKLTC LQNLKWSTAV EFCKKKSCPN PGEIRNGQID VPGGILF GA TISFSCNTGY ...String: (MSE)GCVAETGDC GLPPDVPNAQ PALEGRTSFP EDTVITYKCE ESFVKIPGEK DSVICLKGSQ WSDIEEFCNR SCEVPT RLN SASLKQPYIT QNYFPVGTVV EYECRPGYRR EPSLSPKLTC LQNLKWSTAV EFCKKKSCPN PGEIRNGQID VPGGILF GA TISFSCNTGY KLFGSTSSFC LISGSSVQWS DPLPECREIY CPAPPQIDNG IIQGERDHYG YRQSVTYACN KGFT (MSE)IGEH SIYCTVNNDE GEWSGPPPEC RGGTKHHHHH H UniProtKB: Complement decay-accelerating factor |
-Macromolecule #2: Genome polyprotein
| Macromolecule | Name: Genome polyprotein / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO / EC number: picornain 2A |
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| Source (natural) | Organism: ![]() Echovirus E11 |
| Molecular weight | Theoretical: 28.886428 KDa |
| Recombinant expression | Organism: Homo sapiens (human) |
| Sequence | String: SPSAEECGYS DRVRSITLGN STITTQECAN VVVAYGRWPE YLSDKEATAE DQPTQPDVAT CRFYTLESVT WEKDSPGWWW KFPDALKDM GLFGQNMYYH YLGRAGYTIH VQCNASKFHQ GCLLVVCVPE AEMGCSDVGG TVNEHAISEG EIAKKFSATA T NGAHTVQS ...String: SPSAEECGYS DRVRSITLGN STITTQECAN VVVAYGRWPE YLSDKEATAE DQPTQPDVAT CRFYTLESVT WEKDSPGWWW KFPDALKDM GLFGQNMYYH YLGRAGYTIH VQCNASKFHQ GCLLVVCVPE AEMGCSDVGG TVNEHAISEG EIAKKFSATA T NGAHTVQS IVTNAGMGVG VGNLTIYPHQ WVNLRTNNSA TIVMPYINSV PMDNMFRHHN FTLMIIPFVS LDYSSDASTY VP ITVTVAP MCAEYNGLRL ATSLQ UniProtKB: Genome polyprotein |
-Macromolecule #3: Genome polyprotein
| Macromolecule | Name: Genome polyprotein / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO / EC number: picornain 2A |
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| Source (natural) | Organism: ![]() Echovirus E11 |
| Molecular weight | Theoretical: 26.029674 KDa |
| Recombinant expression | Organism: Homo sapiens (human) |
| Sequence | String: GLPVMNTPGS NQFLTSDDFQ SPSAMPQFDV TPELDIPGEV KNLMEIAEVD SVVPVNNVVG KLDTMDIFRI PVQSGNHQST QVFGFQVQP GLDSVFKHTL LGEILNYYAH WSGSVKLTFV FCGSAMATGK FLLAYSPPGA NAPKTRKDAM LGTHVIWDVG L QSSCVLCI ...String: GLPVMNTPGS NQFLTSDDFQ SPSAMPQFDV TPELDIPGEV KNLMEIAEVD SVVPVNNVVG KLDTMDIFRI PVQSGNHQST QVFGFQVQP GLDSVFKHTL LGEILNYYAH WSGSVKLTFV FCGSAMATGK FLLAYSPPGA NAPKTRKDAM LGTHVIWDVG L QSSCVLCI PWISQTHYRL VHQDEYTSAG NVTCWYQTGI VVPAGTPTLC SIMCFVSACN DFSVRLLKDT PFIEQSALLQ UniProtKB: Genome polyprotein |
-Macromolecule #4: Genome polyprotein
| Macromolecule | Name: Genome polyprotein / type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO / EC number: picornain 2A |
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| Source (natural) | Organism: ![]() Echovirus E11 |
| Molecular weight | Theoretical: 32.284262 KDa |
| Recombinant expression | Organism: Homo sapiens (human) |
| Sequence | String: GDVVEAIEGA VARVADTISS GPTNSQAVPA LTAVETGHTS QVVPGDTMQT RHVKNYHSRS ESTIENFLSR SACVYMGEYY TTNTDETKR FASWTINARR MVQMRRKLEM FTYVRFDVEV TFVITSKQDQ GTQLGQDMPP LTHQIMYIPP GGPIPKSTTD Y AWQTSTNP ...String: GDVVEAIEGA VARVADTISS GPTNSQAVPA LTAVETGHTS QVVPGDTMQT RHVKNYHSRS ESTIENFLSR SACVYMGEYY TTNTDETKR FASWTINARR MVQMRRKLEM FTYVRFDVEV TFVITSKQDQ GTQLGQDMPP LTHQIMYIPP GGPIPKSTTD Y AWQTSTNP SIFWTEGNAP PRMSIPFVSI GNAYSNFYDG WSHFSQNGVY GYNTLNNMGQ LYMRHVNGPS PLPMTSIVRV YF KPKHVKA WVPRPPRLCQ YKNASTVNFS STNITDKRDS ITHVPDTVKP UniProtKB: Genome polyprotein |
-Macromolecule #5: SPHINGOSINE
| Macromolecule | Name: SPHINGOSINE / type: ligand / ID: 5 / Number of copies: 1 / Formula: SPH |
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| Molecular weight | Theoretical: 299.492 Da |
| Chemical component information | ![]() ChemComp-SPH: |
-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: 7.4 |
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| Vitrification | Cryogen name: ETHANE-PROPANE |
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Electron microscopy
| Microscope | FEI TITAN KRIOS |
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| Image recording | Film or detector model: FEI FALCON IV (4k x 4k) / Average electron dose: 41.0 e/Å2 |
| Electron beam | Acceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN |
| Electron optics | Illumination mode: SPOT SCAN / Imaging mode: DARK FIELD / Nominal defocus max: 3.0 µm / Nominal defocus min: 1.0 µm |
| Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Image processing
| Startup model | Type of model: PDB ENTRY PDB model - PDB ID: |
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| Final reconstruction | Resolution.type: BY AUTHOR / Resolution: 3.93 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 201358 |
| Initial angle assignment | Type: MAXIMUM LIKELIHOOD |
| Final angle assignment | Type: MAXIMUM LIKELIHOOD |
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Keywords
Echovirus E11
Homo sapiens (human)
Authors
United Kingdom, 1 items
Citation










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FIELD EMISSION GUN

