[English] 日本語
Yorodumi- PDB-7upn: Maedi visna virus Vif in complex with CypA and E3 ubiquitin ligase -
+Open data
-Basic information
Entry | Database: PDB / ID: 7upn | ||||||
---|---|---|---|---|---|---|---|
Title | Maedi visna virus Vif in complex with CypA and E3 ubiquitin ligase | ||||||
Components |
| ||||||
Keywords | ISOMERASE/VIRAL PROTEIN / virus-host interacting complex / ISOMERASE-VIRAL PROTEIN complex | ||||||
Function / homology | Function and homology information 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 / virion binding / leukocyte chemotaxis / endothelial cell activation / Cul5-RING ubiquitin ligase complex / negative regulation of stress-activated MAPK cascade / Basigin interactions / 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 / protein peptidyl-prolyl isomerization / 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 / Formation of HIV elongation complex in the absence of HIV Tat / positive regulation of viral genome replication / RNA Polymerase II Transcription Elongation / negative regulation of oxidative stress-induced intrinsic apoptotic signaling pathway / Formation of RNA Pol II elongation complex / : / RNA Polymerase II Pre-transcription Events / neutrophil chemotaxis / activation of protein kinase B activity / Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulation / transcription corepressor binding / negative regulation of protein phosphorylation / peptidylprolyl isomerase / peptidyl-prolyl cis-trans isomerase activity / positive regulation of protein secretion / transcription initiation at RNA polymerase II promoter / TP53 Regulates Transcription of DNA Repair Genes / transcription elongation by RNA polymerase II / Vif-mediated degradation of APOBEC3G / negative regulation of protein kinase activity / Assembly Of The HIV Virion / Budding and maturation of HIV virion / Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha / Inactivation of CSF3 (G-CSF) signaling / Evasion by RSV of host interferon responses / neuron differentiation / platelet activation / platelet aggregation / Regulation of expression of SLITs and ROBOs / virion component / integrin binding / SARS-CoV-1 activates/modulates innate immune responses / unfolded protein binding / positive regulation of proteasomal ubiquitin-dependent protein catabolic process / Antigen processing: Ubiquitination & Proteasome degradation / protein folding / Platelet degranulation / Neddylation / positive regulation of NF-kappaB transcription factor activity / protein-macromolecule adaptor 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 / protein ubiquitination / positive regulation of protein phosphorylation / focal adhesion / ubiquitin protein ligase binding / regulation of transcription by RNA polymerase II / Neutrophil degranulation / apoptotic process / protein-containing complex / RNA binding / extracellular space / extracellular exosome / extracellular region / nucleoplasm / membrane / nucleus / cytoplasm / cytosol Similarity search - Function | ||||||
Biological species | Homo sapiens (human) Visna-maedi virus | ||||||
Method | ELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.5 Å | ||||||
Authors | Hu, Y. / Xiong, Y. | ||||||
Funding support | United States, 1items
| ||||||
Citation | Journal: Sci Adv / Year: 2023 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 |
|
-Structure visualization
Structure viewer | Molecule: MolmilJmol/JSmol |
---|
-Downloads & links
-Download
PDBx/mmCIF format | 7upn.cif.gz | 204 KB | Display | PDBx/mmCIF format |
---|---|---|---|---|
PDB format | pdb7upn.ent.gz | 162.2 KB | Display | PDB format |
PDBx/mmJSON format | 7upn.json.gz | Tree view | PDBx/mmJSON format | |
Others | Other downloads |
-Validation report
Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/up/7upn ftp://data.pdbj.org/pub/pdb/validation_reports/up/7upn | HTTPS FTP |
---|
-Related structure data
Related structure data | 26673MC M: map data used to model this data C: citing same article (ref.) |
---|---|
Similar structure data | Similarity search - Function & homologyF&H Search |
-Links
-Assembly
Deposited unit |
|
---|---|
1 |
|
-Components
#1: Protein | Mass: 18036.504 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: PPIA, CYPA / Production host: Escherichia coli (E. coli) / References: UniProt: P62937, peptidylprolyl isomerase #2: Protein | Mass: 28182.600 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Visna-maedi virus / Strain: KV1772 / Gene: vif / Production host: Escherichia coli (E. coli) / References: UniProt: P69717 #3: Protein | Mass: 10843.420 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: ELOC, TCEB1 / Production host: Escherichia coli (E. coli) / References: UniProt: Q15369 #4: Protein | Mass: 13147.781 Da / Num. of mol.: 2 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: ELOB, TCEB2 / Production host: Escherichia coli (E. coli) / References: UniProt: Q15370 #5: Chemical | Has ligand of interest | Y | |
---|
-Experimental details
-Experiment
Experiment | Method: ELECTRON MICROSCOPY |
---|---|
EM experiment | Aggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction |
-Sample preparation
Component | Name: Maedi visna virus Vif in complex with human CypA and Elongin BC components of E3 ubiquitin ligase Type: COMPLEX / Entity ID: #1-#4 / Source: RECOMBINANT |
---|---|
Source (natural) | Organism: Homo sapiens (human) |
Source (recombinant) | Organism: Escherichia coli (E. coli) |
Buffer solution | pH: 7.2 |
Specimen | Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
Specimen support | Grid material: COPPER / Grid type: C-flat-2/1 |
Vitrification | Cryogen name: ETHANE |
-Electron microscopy imaging
Experimental equipment | Model: Titan Krios / Image courtesy: FEI Company |
---|---|
Microscopy | Model: FEI TITAN KRIOS |
Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM |
Electron lens | Mode: BRIGHT FIELD / Nominal defocus max: 2000 nm / Nominal defocus min: 900 nm |
Image recording | Electron dose: 62 e/Å2 / Film or detector model: GATAN K3 (6k x 4k) |
-Processing
Software | Name: PHENIX / Version: 1.19.2_4158: / Classification: refinement | ||||||||||||||||||||||||
---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
CTF correction | Type: NONE | ||||||||||||||||||||||||
Symmetry | Point symmetry: C2 (2 fold cyclic) | ||||||||||||||||||||||||
3D reconstruction | Resolution: 3.5 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 74320 / Symmetry type: POINT | ||||||||||||||||||||||||
Refine LS restraints |
|