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Yorodumi- PDB-6gk2: Helical reconstruction of BCL10 CARD and MALT1 DEATH DOMAIN complex -
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Open data
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Basic information
| Entry | Database: PDB / ID: 6gk2 | ||||||
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| Title | Helical reconstruction of BCL10 CARD and MALT1 DEATH DOMAIN complex | ||||||
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Keywords | IMMUNE SYSTEM / BCL10 / MALT1 / CBM complex / helical reconstruction / cancer / autoimmune disease | ||||||
| Function / homology | Function and homology informationpositive regulation of lymphotoxin A production / polkadots / B-1 B cell differentiation / positive regulation of T-helper 17 cell differentiation / CBM complex / regulation of T cell receptor signaling pathway / protein kinase B binding / antifungal innate immune response / response to fungus / CARD domain binding ...positive regulation of lymphotoxin A production / polkadots / B-1 B cell differentiation / positive regulation of T-helper 17 cell differentiation / CBM complex / regulation of T cell receptor signaling pathway / protein kinase B binding / antifungal innate immune response / response to fungus / CARD domain binding / positive regulation of mast cell cytokine production / T cell apoptotic process / negative regulation of mature B cell apoptotic process / CLEC7A/inflammasome pathway / programmed cell death / B cell apoptotic process / nuclear export / non-canonical NF-kappaB signal transduction / positive regulation of extrinsic apoptotic signaling pathway / toll-like receptor signaling pathway / response to food / small molecule binding / positive regulation of T cell receptor signaling pathway / B cell activation / immunoglobulin mediated immune response / general transcription initiation factor binding / immunological synapse / positive regulation of phosphorylation / NF-kappaB binding / endopeptidase activator activity / cellular defense response / T cell proliferation / cytoplasmic microtubule / signaling adaptor activity / positive regulation of interleukin-2 production / proteolysis involved in protein catabolic process / lipopolysaccharide-mediated signaling pathway / positive regulation of interleukin-1 beta production / positive regulation of protein ubiquitination / positive regulation of interleukin-8 production / neural tube closure / apoptotic signaling pathway / Activation of NF-kappaB in B cells / cellular response to mechanical stimulus / positive regulation of NF-kappaB transcription factor activity / defense response / positive regulation of T cell cytokine production / protein homooligomerization / positive regulation of T cell activation / positive regulation of interleukin-6 production / CLEC7A (Dectin-1) signaling / FCERI mediated NF-kB activation / fibrillar center / ubiquitin-protein transferase activity / Downstream TCR signaling / peptidase activity / T cell receptor signaling pathway / E3 ubiquitin ligases ubiquitinate target proteins / cellular response to lipopolysaccharide / protease binding / protein-macromolecule adaptor activity / regulation of apoptotic process / endopeptidase activity / adaptive immune response / transcription coactivator activity / Hydrolases; Acting on peptide bonds (peptidases); Cysteine endopeptidases / lysosome / positive regulation of canonical NF-kappaB signal transduction / positive regulation of apoptotic process / membrane raft / innate immune response / cysteine-type endopeptidase activity / ubiquitin protein ligase binding / negative regulation of apoptotic process / protein-containing complex binding / positive regulation of DNA-templated transcription / perinuclear region of cytoplasm / protein-containing complex / proteolysis / nucleoplasm / identical protein binding / nucleus / cytosol / cytoplasm Similarity search - Function | ||||||
| Biological species | Homo sapiens (human) | ||||||
| Method | ELECTRON MICROSCOPY / helical reconstruction / cryo EM / Resolution: 4.9 Å | ||||||
Authors | Schlauderer, F. / Desfosses, A. / Gutsche, I. / Hopfner, K.P. / Lammens, K. | ||||||
Citation | Journal: Nat Commun / Year: 2018Title: Molecular architecture and regulation of BCL10-MALT1 filaments. Authors: Florian Schlauderer / Thomas Seeholzer / Ambroise Desfosses / Torben Gehring / Mike Strauss / Karl-Peter Hopfner / Irina Gutsche / Daniel Krappmann / Katja Lammens / ![]() Abstract: The CARD11-BCL10-MALT1 (CBM) complex triggers the adaptive immune response in lymphocytes and lymphoma cells. CARD11/CARMA1 acts as a molecular seed inducing BCL10 filaments, but the integration of ...The CARD11-BCL10-MALT1 (CBM) complex triggers the adaptive immune response in lymphocytes and lymphoma cells. CARD11/CARMA1 acts as a molecular seed inducing BCL10 filaments, but the integration of MALT1 and the assembly of a functional CBM complex has remained elusive. Using cryo-EM we solved the helical structure of the BCL10-MALT1 filament. The structural model of the filament core solved at 4.9 Å resolution identified the interface between the N-terminal MALT1 DD and the BCL10 caspase recruitment domain. The C-terminal MALT1 Ig and paracaspase domains protrude from this core to orchestrate binding of mediators and substrates at the filament periphery. Mutagenesis studies support the importance of the identified BCL10-MALT1 interface for CBM complex assembly, MALT1 protease activation and NF-κB signaling in Jurkat and primary CD4 T-cells. Collectively, we present a model for the assembly and architecture of the CBM signaling complex and how it functions as a signaling hub in T-lymphocytes. | ||||||
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Structure visualization
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| Structure viewer | Molecule: Molmil Jmol/JSmol |
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Downloads & links
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Download
| PDBx/mmCIF format | 6gk2.cif.gz | 45.8 KB | Display | PDBx/mmCIF format |
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| PDB format | pdb6gk2.ent.gz | 31.5 KB | Display | PDB format |
| PDBx/mmJSON format | 6gk2.json.gz | Tree view | PDBx/mmJSON format | |
| Others | Other downloads |
-Validation report
| Summary document | 6gk2_validation.pdf.gz | 1.1 MB | Display | wwPDB validaton report |
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| Full document | 6gk2_full_validation.pdf.gz | 1.1 MB | Display | |
| Data in XML | 6gk2_validation.xml.gz | 14.5 KB | Display | |
| Data in CIF | 6gk2_validation.cif.gz | 16.3 KB | Display | |
| Arichive directory | https://data.pdbj.org/pub/pdb/validation_reports/gk/6gk2 ftp://data.pdbj.org/pub/pdb/validation_reports/gk/6gk2 | HTTPS FTP |
-Related structure data
| Related structure data | ![]() 0013MC M: map data used to model this data C: citing same article ( |
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| Similar structure data |
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Links
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Assembly
| Deposited unit | ![]()
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Components
| #1: Protein | Mass: 12614.566 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: BCL10, CIPER, CLAP / Production host: ![]() |
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| #2: Protein | Mass: 10401.128 Da / Num. of mol.: 1 Source method: isolated from a genetically manipulated source Source: (gene. exp.) Homo sapiens (human) / Gene: MALT1, MLT / Production host: ![]() References: UniProt: Q9UDY8, Hydrolases; Acting on peptide bonds (peptidases); Cysteine endopeptidases |
| Has protein modification | Y |
-Experimental details
-Experiment
| Experiment | Method: ELECTRON MICROSCOPY |
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| EM experiment | Aggregation state: FILAMENT / 3D reconstruction method: helical reconstruction |
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Sample preparation
| Component | Name: Complex of BCL10 CARD and MALT1 DEATH DOMAIN / Type: COMPLEX / Entity ID: all / Source: RECOMBINANT |
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| Molecular weight | Value: 104 kDa/nm / Experimental value: YES |
| Source (natural) | Organism: Homo sapiens (human) |
| Source (recombinant) | Organism: ![]() |
| Buffer solution | pH: 7.5 |
| Specimen | Conc.: 1 mg/ml / Embedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES |
| Specimen support | Grid material: COPPER / Grid type: Quantifoil R1.2/1.3 |
| Vitrification | Cryogen name: ETHANE |
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Electron microscopy imaging
| Experimental equipment | ![]() Model: Talos Arctica / Image courtesy: FEI Company |
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| Microscopy | Model: FEI TECNAI ARCTICA |
| Electron gun | Electron source: FIELD EMISSION GUN / Accelerating voltage: 200 kV / Illumination mode: FLOOD BEAM |
| Electron lens | Mode: BRIGHT FIELD |
| Image recording | Electron dose: 99.6 e/Å2 / Detector mode: INTEGRATING / Film or detector model: FEI FALCON III (4k x 4k) |
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Processing
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| CTF correction | Type: NONE | ||||||||||||||||||||||||
| Helical symmerty | Angular rotation/subunit: -100.8 ° / Axial rise/subunit: 5.082 Å / Axial symmetry: C1 | ||||||||||||||||||||||||
| Particle selection | Num. of particles selected: 25776 | ||||||||||||||||||||||||
| 3D reconstruction | Resolution: 4.9 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 9600 / Symmetry type: HELICAL |
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Homo sapiens (human)
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FIELD EMISSION GUN