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- EMDB-26673: Maedi visna virus Vif in complex with CypA and E3 ubiquitin ligase -
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Open data
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Basic information
Entry | ![]() | |||||||||
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Title | Maedi visna virus Vif in complex with CypA and E3 ubiquitin ligase | |||||||||
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![]() | virus-host interacting complex / ISOMERASE-VIRAL PROTEIN complex | |||||||||
Function / homology | ![]() negative regulation of protein K48-linked ubiquitination / negative regulation of viral life cycle / regulation of apoptotic signaling pathway / cell adhesion molecule production / lipid droplet organization / target-directed miRNA degradation / elongin complex / heparan sulfate binding / regulation of viral genome replication / VCB complex ...negative regulation of protein K48-linked ubiquitination / negative regulation of viral life cycle / regulation of apoptotic signaling pathway / cell adhesion molecule production / lipid droplet organization / target-directed miRNA degradation / elongin complex / heparan sulfate binding / regulation of viral genome replication / VCB complex / leukocyte chemotaxis / endothelial cell activation / virion binding / Cul5-RING ubiquitin ligase complex / Basigin interactions / negative regulation of stress-activated MAPK cascade / Cul2-RING ubiquitin ligase complex / cyclosporin A binding / Minus-strand DNA synthesis / Plus-strand DNA synthesis / Uncoating of the HIV Virion / Early Phase of HIV Life Cycle / Integration of provirus / APOBEC3G mediated resistance to HIV-1 infection / Pausing and recovery of Tat-mediated HIV elongation / Tat-mediated HIV elongation arrest and recovery / HIV elongation arrest and recovery / Pausing and recovery of HIV elongation / Calcineurin activates NFAT / viral release from host cell / Tat-mediated elongation of the HIV-1 transcript / Formation of HIV-1 elongation complex containing HIV-1 Tat / Binding and entry of HIV virion / positive regulation of viral genome replication / Formation of HIV elongation complex in the absence of HIV Tat / protein peptidyl-prolyl isomerization / RNA Polymerase II Transcription Elongation / negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway / Formation of RNA Pol II elongation complex / positive regulation of protein dephosphorylation / RNA Polymerase II Pre-transcription Events / Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulation / activation of protein kinase B activity / neutrophil chemotaxis / transcription corepressor binding / negative regulation of protein phosphorylation / peptidylprolyl isomerase / virion component / peptidyl-prolyl cis-trans isomerase activity / transcription elongation by RNA polymerase II / positive regulation of protein secretion / TP53 Regulates Transcription of DNA Repair Genes / transcription initiation at RNA polymerase II promoter / Vif-mediated degradation of APOBEC3G / Assembly Of The HIV Virion / negative regulation of protein kinase activity / Budding and maturation of HIV virion / Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha / neuron differentiation / Inactivation of CSF3 (G-CSF) signaling / Evasion by RSV of host interferon responses / platelet activation / platelet aggregation / Regulation of expression of SLITs and ROBOs / SARS-CoV-1 activates/modulates innate immune responses / unfolded protein binding / Antigen processing: Ubiquitination & Proteasome degradation / positive regulation of proteasomal ubiquitin-dependent protein catabolic process / integrin binding / protein folding / Platelet degranulation / protein-macromolecule adaptor activity / Neddylation / positive regulation of NF-kappaB transcription factor activity / cellular response to oxidative stress / ubiquitin-dependent protein catabolic process / protein-containing complex assembly / secretory granule lumen / vesicle / ficolin-1-rich granule lumen / host cell cytoplasm / positive regulation of MAPK cascade / response to hypoxia / protein ubiquitination / positive regulation of protein phosphorylation / focal adhesion / apoptotic process / ubiquitin protein ligase binding / Neutrophil degranulation / regulation of transcription by RNA polymerase II / protein-containing complex / RNA binding / extracellular space / extracellular exosome / extracellular region / nucleoplasm / membrane / nucleus / cytoplasm / cytosol Similarity search - Function | |||||||||
Biological species | ![]() ![]() | |||||||||
Method | single particle reconstruction / cryo EM / Resolution: 3.5 Å | |||||||||
![]() | Hu Y / Xiong Y | |||||||||
Funding support | ![]()
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![]() | ![]() Title: Structural basis for recruitment of host CypA and E3 ubiquitin ligase by maedi-visna virus Vif. Authors: Yingxia Hu / Ragna B Gudnadóttir / Kirsten M Knecht / Fidel Arizaga / Stefán R Jónsson / Yong Xiong / ![]() ![]() Abstract: Lentiviral Vif molecules target the host antiviral APOBEC3 proteins for destruction in cellular ubiquitin-proteasome pathways. Different lentiviral Vifs have evolved to use the same canonical E3 ...Lentiviral Vif molecules target the host antiviral APOBEC3 proteins for destruction in cellular ubiquitin-proteasome pathways. Different lentiviral Vifs have evolved to use the same canonical E3 ubiquitin ligase complexes, along with distinct noncanonical host cofactors for their activities. Unlike primate lentiviral Vif, which recruits CBFβ as the noncanonical cofactor, nonprimate lentiviral Vif proteins have developed different cofactor recruitment mechanisms. Maedi-visna virus (MVV) sequesters CypA as the noncanonical cofactor for the Vif-mediated ubiquitination of ovine APOBEC3s. Here, we report the cryo-electron microscopy structure of MVV Vif in complex with CypA and E3 ligase components. The structure, along with our biochemical and functional analysis, reveals both conserved and unique structural elements of MVV Vif and its common and distinct interaction modes with various cognate cellular proteins, providing a further understanding of the evolutionary relationship between lentiviral Vifs and the molecular mechanisms by which they capture different host cofactors for immune evasion activities. | |||||||||
History |
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Structure visualization
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 21.5 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 17.4 KB 17.4 KB | Display Display | ![]() |
Images | ![]() | 47.5 KB | ||
Filedesc metadata | ![]() | 5.7 KB | ||
Others | ![]() ![]() | 39.7 MB 39.7 MB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 815.6 KB | Display | ![]() |
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Full document | ![]() | 815.1 KB | Display | |
Data in XML | ![]() | 11.4 KB | Display | |
Data in CIF | ![]() | 13.3 KB | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
Related structure data | ![]() 7upnMC M: atomic model generated by this map C: citing same article ( |
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Similar structure data | Similarity search - Function & homology ![]() |
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Links
EMDB pages | ![]() ![]() |
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Related items in Molecule of the Month |
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Map
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Voxel size | X=Y=Z: 1.1 Å | ||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||
Details | EMDB XML:
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-Supplemental data
-Half map: #2
File | emd_26673_half_map_1.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
-Half map: #1
File | emd_26673_half_map_2.map | ||||||||||||
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Projections & Slices |
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Density Histograms |
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Sample components
-Entire : Maedi visna virus Vif in complex with human CypA and Elongin BC c...
Entire | Name: Maedi visna virus Vif in complex with human CypA and Elongin BC components of E3 ubiquitin ligase |
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Components |
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-Supramolecule #1: Maedi visna virus Vif in complex with human CypA and Elongin BC c...
Supramolecule | Name: Maedi visna virus Vif in complex with human CypA and Elongin BC components of E3 ubiquitin ligase type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#4 |
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Source (natural) | Organism: ![]() |
-Macromolecule #1: Peptidyl-prolyl cis-trans isomerase A
Macromolecule | Name: Peptidyl-prolyl cis-trans isomerase A / type: protein_or_peptide / ID: 1 / Number of copies: 2 / Enantiomer: LEVO / EC number: peptidylprolyl isomerase |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 18.036504 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: MVNPTVFFDI AVDGEPLGRV SFELFADKVP KTAENFRALS TGEKGFGYKG SCFHRIIPGF MCQGGDFTRH NGTGGKSIYG EKFEDENFI LKHTGPGILS MANAGPNTNG SQFFICTAKT EWLDGKHVVF GKVKEGMNIV EAMERFGSRN GKTSKKITIA D CGQLE UniProtKB: Peptidyl-prolyl cis-trans isomerase A |
-Macromolecule #2: Virion infectivity factor
Macromolecule | Name: Virion infectivity factor / type: protein_or_peptide / ID: 2 / Number of copies: 2 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 28.1826 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: MLSSYRHQKK YKKNKAREIG PQLPLWAWKE TAFSINQEPY WYSTIRLQGL MWNKRGHKLM FVKENQGYEY WETSGKQWKM EIRRDLDLI AQINFRNAWQ YKSQGEWKTI GVWYESPGDY KGKENQFWFH WRIALCSCNK TRWDIREFMI GKHRWDLCKS C IQGEIVKN ...String: MLSSYRHQKK YKKNKAREIG PQLPLWAWKE TAFSINQEPY WYSTIRLQGL MWNKRGHKLM FVKENQGYEY WETSGKQWKM EIRRDLDLI AQINFRNAWQ YKSQGEWKTI GVWYESPGDY KGKENQFWFH WRIALCSCNK TRWDIREFMI GKHRWDLCKS C IQGEIVKN TNPRSLQRLA LLHLAKDHVF QVMPLWRARR VTVQKFPWCR SPMGYTIPWS LQECWEMESI FE UniProtKB: Virion infectivity factor |
-Macromolecule #3: Elongin-C
Macromolecule | Name: Elongin-C / type: protein_or_peptide / ID: 3 / Number of copies: 2 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 10.84342 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: MYVKLISSDG HEFIVKREHA LTSGTIKAML SGPGQFAENE TNEVNFREIP SHVLSKVCMY FTYKVRYTNS STEIPEFPIA PEIALELLM AANFLDC UniProtKB: Elongin-C |
-Macromolecule #4: Elongin-B
Macromolecule | Name: Elongin-B / type: protein_or_peptide / ID: 4 / Number of copies: 2 / Enantiomer: LEVO |
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Source (natural) | Organism: ![]() |
Molecular weight | Theoretical: 13.147781 KDa |
Recombinant expression | Organism: ![]() ![]() |
Sequence | String: MDVFLMIRRH KTTIFTDAKE SSTVFELKRI VEGILKRPPD EQRLYKDDQL LDDGKTLGEC GFTSQTARPQ APATVGLAFR ADDTFEALC IEPFSSPPEL PDVMKPQDSG SSANEQAVQ UniProtKB: Elongin-B |
-Macromolecule #5: ZINC ION
Macromolecule | Name: ZINC ION / type: ligand / ID: 5 / Number of copies: 2 / Formula: ZN |
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Molecular weight | Theoretical: 65.409 Da |
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | single particle reconstruction |
Aggregation state | particle |
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Sample preparation
Buffer | pH: 7.2 |
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Grid | Model: C-flat-2/1 / Material: COPPER / Support film - Material: GRAPHENE |
Vitrification | Cryogen name: ETHANE |
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Electron microscopy
Microscope | FEI TITAN KRIOS |
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Image recording | Film or detector model: GATAN K3 (6k x 4k) / Average electron dose: 62.0 e/Å2 |
Electron beam | Acceleration voltage: 300 kV / Electron source: ![]() |
Electron optics | Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.0 µm / Nominal defocus min: 0.9 µm |
Experimental equipment | ![]() Model: Titan Krios / Image courtesy: FEI Company |
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Image processing
Startup model | Type of model: INSILICO MODEL |
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Final reconstruction | Applied symmetry - Point group: C2 (2 fold cyclic) / Resolution.type: BY AUTHOR / Resolution: 3.5 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 74320 |
Initial angle assignment | Type: MAXIMUM LIKELIHOOD |
Final angle assignment | Type: MAXIMUM LIKELIHOOD |