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- EMDB-5922: 3.6 Angstrom resolution MAVS filament generated from helical reco... -
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Basic information
Entry | Database: EMDB / ID: EMD-5922 | |||||||||
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Title | 3.6 Angstrom resolution MAVS filament generated from helical reconstruction | |||||||||
![]() | 3.6 Angstrom resolution MAVS filament generated from helical reconstruction | |||||||||
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![]() | CARD / MAVS / innate immunity / RIG-I / MDA5 / spontaneous filament formation | |||||||||
Function / homology | ![]() positive regulation of IP-10 production / regulation of peroxisome organization / RIG-I binding / positive regulation of chemokine (C-C motif) ligand 5 production / positive regulation of myeloid dendritic cell cytokine production / CARD domain binding / NF-kB activation through FADD/RIP-1 pathway mediated by caspase-8 and -10 / protein localization to mitochondrion / positive regulation of response to cytokine stimulus / positive regulation of type I interferon-mediated signaling pathway ...positive regulation of IP-10 production / regulation of peroxisome organization / RIG-I binding / positive regulation of chemokine (C-C motif) ligand 5 production / positive regulation of myeloid dendritic cell cytokine production / CARD domain binding / NF-kB activation through FADD/RIP-1 pathway mediated by caspase-8 and -10 / protein localization to mitochondrion / positive regulation of response to cytokine stimulus / positive regulation of type I interferon-mediated signaling pathway / peroxisomal membrane / TRAF6 mediated IRF7 activation / negative regulation of type I interferon-mediated signaling pathway / positive regulation of NLRP3 inflammasome complex assembly / cytoplasmic pattern recognition receptor signaling pathway / negative regulation of viral genome replication / type I interferon-mediated signaling pathway / cellular response to exogenous dsRNA / TRAF6 mediated NF-kB activation / antiviral innate immune response / positive regulation of type I interferon production / positive regulation of interferon-alpha production / signaling adaptor activity / ubiquitin ligase complex / positive regulation of defense response to virus by host / activation of innate immune response / positive regulation of interferon-beta production / molecular condensate scaffold activity / positive regulation of interleukin-8 production / Negative regulators of DDX58/IFIH1 signaling / mitochondrial membrane / DDX58/IFIH1-mediated induction of interferon-alpha/beta / PKR-mediated signaling / Evasion by RSV of host interferon responses / positive regulation of DNA-binding transcription factor activity / positive regulation of protein import into nucleus / SARS-CoV-1 activates/modulates innate immune responses / positive regulation of interleukin-6 production / positive regulation of tumor necrosis factor production / Ovarian tumor domain proteases / TRAF3-dependent IRF activation pathway / positive regulation of canonical NF-kappaB signal transduction / defense response to virus / mitochondrial outer membrane / molecular adaptor activity / defense response to bacterium / positive regulation of protein phosphorylation / innate immune response / protein kinase binding / SARS-CoV-2 activates/modulates innate and adaptive immune responses / signal transduction / positive regulation of transcription by RNA polymerase II / mitochondrion / identical protein binding Similarity search - Function | |||||||||
Biological species | ![]() | |||||||||
Method | helical reconstruction / cryo EM / Resolution: 3.64 Å | |||||||||
![]() | Wu B / Peisley A / Li Z / Egelman E / Walz T / Penczek P / Hur S | |||||||||
![]() | ![]() Title: Molecular imprinting as a signal-activation mechanism of the viral RNA sensor RIG-I. Authors: Bin Wu / Alys Peisley / David Tetrault / Zongli Li / Edward H Egelman / Katharine E Magor / Thomas Walz / Pawel A Penczek / Sun Hur / ![]() ![]() Abstract: RIG-I activates interferon signaling pathways by promoting filament formation of the adaptor molecule, MAVS. Assembly of the MAVS filament is mediated by its CARD domain (CARD(MAVS)), and requires ...RIG-I activates interferon signaling pathways by promoting filament formation of the adaptor molecule, MAVS. Assembly of the MAVS filament is mediated by its CARD domain (CARD(MAVS)), and requires its interaction with the tandem CARDs of RIG-I (2CARD(RIG-I)). However, the precise nature of the interaction between 2CARD(RIG-I) and CARD(MAVS), and how this interaction leads to CARD(MAVS) filament assembly, has been unclear. Here we report a 3.6 Å electron microscopy structure of the CARD(MAVS) filament and a 3.4 Å crystal structure of the 2CARD(RIG-I):CARD(MAVS) complex, representing 2CARD(RIG-I) "caught in the act" of nucleating the CARD(MAVS) filament. These structures, together with functional analyses, show that 2CARD(RIG-I) acts as a template for the CARD(MAVS) filament assembly, by forming a helical tetrameric structure and recruiting CARD(MAVS) along its helical trajectory. Our work thus reveals that signal activation by RIG-I occurs by imprinting its helical assembly architecture on MAVS, a previously uncharacterized mechanism of signal transmission. | |||||||||
History |
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Structure visualization
Movie |
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Structure viewer | EM map: ![]() ![]() ![]() |
Supplemental images |
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Downloads & links
-EMDB archive
Map data | ![]() | 8.1 MB | ![]() | |
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Header (meta data) | ![]() ![]() | 9.5 KB 9.5 KB | Display Display | ![]() |
Images | ![]() ![]() | 95.5 KB 5.9 KB | ||
Archive directory | ![]() ![]() | HTTPS FTP |
-Validation report
Summary document | ![]() | 78.9 KB | Display | ![]() |
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Full document | ![]() | 78 KB | Display | |
Data in XML | ![]() | 493 B | Display | |
Arichive directory | ![]() ![]() | HTTPS FTP |
-Related structure data
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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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Annotation | 3.6 Angstrom resolution MAVS filament generated from helical reconstruction | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Voxel size | X=Y=Z: 0.62 Å | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Density |
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Symmetry | Space group: 1 | ||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||||
Details | EMDB XML:
CCP4 map header:
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-Supplemental data
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Sample components
-Entire : MAVS filament
Entire | Name: MAVS filament |
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Components |
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-Supramolecule #1000: MAVS filament
Supramolecule | Name: MAVS filament / type: sample / ID: 1000 / Details: The density is only a section of the filament. / Oligomeric state: filament / Number unique components: 1 |
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Molecular weight | Experimental: 150 KDa / Theoretical: 150 KDa / Method: Size exclusion chromatography |
-Macromolecule #1: Mitochondria Anti-viral Signaling protein, CARD domain
Macromolecule | Name: Mitochondria Anti-viral Signaling protein, CARD domain type: protein_or_peptide / ID: 1 / Name.synonym: MAVS / Oligomeric state: filament / Recombinant expression: Yes |
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Source (natural) | Organism: ![]() |
Recombinant expression | Organism: ![]() ![]() |
Sequence | UniProtKB: Mitochondrial antiviral-signaling protein |
-Experimental details
-Structure determination
Method | cryo EM |
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![]() | helical reconstruction |
Aggregation state | filament |
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Sample preparation
Concentration | 0.2 mg/mL |
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Buffer | pH: 7.5 / Details: 20 mM Tris, 150 mM NaCl |
Grid | Details: glow-discharged Quantifoil R1.2/1.3 holey carbon grids |
Vitrification | Cryogen name: NITROGEN / Instrument: FEI VITROBOT MARK I |
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Electron microscopy
Microscope | FEI TECNAI F20 |
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Specialist optics | Energy filter - Name: FEI |
Details | Movies were recorded at liquid nitrogen temperature with a K2 Summit direct detector device camera operated in super-resolution mode with dose-fractionation. |
Date | Aug 10, 2013 |
Image recording | Category: CCD / Film or detector model: GATAN K2 (4k x 4k) / Number real images: 1863 / Average electron dose: 31 e/Å2 |
Electron beam | Acceleration voltage: 200 kV / Electron source: ![]() |
Electron optics | Calibrated magnification: 40410 / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal magnification: 29000 |
Sample stage | Specimen holder model: GATAN LIQUID NITROGEN |
Experimental equipment | ![]() Model: Tecnai F20 / Image courtesy: FEI Company |
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Image processing
Details | The electron density map of the filament was reconstructed using a helical geometrically constrained reconstruction approach (Helicon). |
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Final reconstruction | Applied symmetry - Helical parameters - Δz: 5.13 Å Applied symmetry - Helical parameters - Δ&Phi: 101.1 ° Applied symmetry - Helical parameters - Axial symmetry: C1 (asymmetric) Resolution.type: BY AUTHOR / Resolution: 3.64 Å / Resolution method: OTHER / Software - Name: Helicon |