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- EMDB-0013: Helical reconstruction of BCL10 CARD and MALT1 DEATH DOMAIN complex -

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Basic information

Entry
Database: EMDB / ID: EMD-0013
TitleHelical reconstruction of BCL10 CARD and MALT1 DEATH DOMAIN complex
Map data
Sample
  • Complex: Complex of BCL10 CARD and MALT1 DEATH DOMAIN
    • Protein or peptide: B-cell lymphoma/leukemia 10
    • Protein or peptide: Mucosa-associated lymphoid tissue lymphoma translocation protein 1
KeywordsBCL10 / MALT1 / CBM complex / helical reconstruction / cancer / autoimmune disease / IMMUNE SYSTEM
Function / homology
Function and homology information


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 / positive regulation of mast cell cytokine production ...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 / positive regulation of mast cell cytokine production / CARD domain binding / T cell apoptotic process / negative regulation of mature B cell apoptotic process / B cell apoptotic process / CLEC7A/inflammasome pathway / programmed cell death / nuclear export / positive regulation of extrinsic apoptotic signaling pathway / non-canonical NF-kappaB signal transduction / response to food / toll-like receptor signaling pathway / positive regulation of T cell receptor signaling pathway / small molecule binding / B cell activation / immunoglobulin mediated immune response / immunological synapse / general transcription initiation factor binding / endopeptidase activator activity / NF-kappaB binding / cellular defense response / positive regulation of phosphorylation / T cell proliferation / cytoplasmic microtubule / signaling adaptor activity / positive regulation of interleukin-2 production / lipopolysaccharide-mediated signaling pathway / proteolysis involved in protein catabolic process / 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 / defense response / positive regulation of T cell cytokine production / protein homooligomerization / positive regulation of interleukin-6 production / CLEC7A (Dectin-1) signaling / positive regulation of T cell activation / FCERI mediated NF-kB activation / fibrillar center / cellular response to mechanical stimulus / positive regulation of NF-kappaB transcription factor activity / ubiquitin-protein transferase activity / Downstream TCR signaling / E3 ubiquitin ligases ubiquitinate target proteins / peptidase activity / T cell receptor signaling pathway / cellular response to lipopolysaccharide / protease binding / protein-macromolecule adaptor activity / regulation of apoptotic process / endopeptidase activity / adaptive immune response / positive regulation of canonical NF-kappaB signal transduction / transcription coactivator activity / Hydrolases; Acting on peptide bonds (peptidases); Cysteine endopeptidases / lysosome / positive regulation of apoptotic process / membrane raft / innate immune response / cysteine-type endopeptidase activity / ubiquitin protein ligase binding / protein-containing complex binding / negative regulation of apoptotic process / positive regulation of DNA-templated transcription / perinuclear region of cytoplasm / protein-containing complex / proteolysis / nucleoplasm / identical protein binding / nucleus / cytosol / cytoplasm
Similarity search - Function
B-cell lymphoma/leukemia 10/E10 / BCL10, CARD domain / Mucosa-associated lymphoid tissue lymphoma translocation protein 1 / MALT1, death domain / MALT1 immunoglobulin-like domain / : / MALT1 Ig-like domain / CARD domain / CARD caspase recruitment domain profile. / Caspase recruitment domain ...B-cell lymphoma/leukemia 10/E10 / BCL10, CARD domain / Mucosa-associated lymphoid tissue lymphoma translocation protein 1 / MALT1, death domain / MALT1 immunoglobulin-like domain / : / MALT1 Ig-like domain / CARD domain / CARD caspase recruitment domain profile. / Caspase recruitment domain / Immunoglobulin domain / Peptidase C14, p20 domain / Caspase family p20 domain profile. / : / Caspase domain / Caspase-like domain superfamily / Immunoglobulin domain / Death-like domain superfamily / Immunoglobulin subtype 2 / Immunoglobulin C-2 Type / Immunoglobulin subtype / Immunoglobulin / Ig-like domain profile. / Immunoglobulin-like domain / Immunoglobulin-like domain superfamily / Immunoglobulin-like fold
Similarity search - Domain/homology
B-cell lymphoma/leukemia 10 / Mucosa-associated lymphoid tissue lymphoma translocation protein 1
Similarity search - Component
Biological speciesHomo sapiens (human)
Methodhelical reconstruction / cryo EM / Resolution: 4.9 Å
AuthorsSchlauderer F / Desfosses A
CitationJournal: Nat Commun / Year: 2018
Title: 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.
History
DepositionMay 18, 2018-
Header (metadata) releaseOct 31, 2018-
Map releaseOct 31, 2018-
UpdateNov 6, 2024-
Current statusNov 6, 2024Processing site: PDBe / Status: Released

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Structure visualization

Structure viewerEM map:
SurfViewMolmilJmol/JSmol
Supplemental images

emd_0013.png

Downloads & links

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Map

FileDownload / File: emd_0013.map.gz / Format: CCP4 / Size: 91.6 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
1 Å/pix.
x 250 pix.
= 250.5 Å		1 Å/pix.
x 310 pix.
= 310.62 Å		1 Å/pix.
x 310 pix.
= 310.62 Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

generated in cubic-lattice coordinate

Voxel sizeX=Y=Z: 1.002 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 2.0 / Movie #1: 0
Minimum - Maximum-3.856203 - 7.497551
Average (Standard dev.)0.019812632 (±0.63959557)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin-155-155-125
Dimensions310310250
Spacing310310250
CellA: 310.62 Å / B: 310.62 Å / C: 250.5 Å
α=β=γ: 90.0 °

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Supplemental data

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Half map: Unmasked, unfiltered, helically symmetrized half map 2

Fileemd_0013_half_map_1.map
AnnotationUnmasked, unfiltered, helically symmetrized half map 2
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Half map: Unmasked, unfiltered, helically symmetrized half map 1

Fileemd_0013_half_map_2.map
AnnotationUnmasked, unfiltered, helically symmetrized half map 1
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Sample components

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Entire : Complex of BCL10 CARD and MALT1 DEATH DOMAIN

EntireName: Complex of BCL10 CARD and MALT1 DEATH DOMAIN
Components
  • Complex: Complex of BCL10 CARD and MALT1 DEATH DOMAIN
    • Protein or peptide: B-cell lymphoma/leukemia 10
    • Protein or peptide: Mucosa-associated lymphoid tissue lymphoma translocation protein 1

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Supramolecule #1: Complex of BCL10 CARD and MALT1 DEATH DOMAIN

SupramoleculeName: Complex of BCL10 CARD and MALT1 DEATH DOMAIN / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 104 kDa/nm

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Macromolecule #1: B-cell lymphoma/leukemia 10

MacromoleculeName: B-cell lymphoma/leukemia 10 / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 12.614566 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString:
EEDLTEVKKD ALENLRVYLC EKIIAERHFD HLRAKKILSR EDTEEISCRT SSRKRAGKLL DYLQENPKGL DTLVESIRRE KTQNFLIQK ITDEVLKLRN IKLEHLK

UniProtKB: B-cell lymphoma/leukemia 10

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Macromolecule #2: Mucosa-associated lymphoid tissue lymphoma translocation protein 1

MacromoleculeName: Mucosa-associated lymphoid tissue lymphoma translocation protein 1
type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO
EC number: Hydrolases; Acting on peptide bonds (peptidases); Cysteine endopeptidases
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 10.401128 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString:
LNRLREPLLR RLSELLDQAP EGRGWRRLAE LAGSRGRLRL SCLDLEQCSL KVLEPEGSPS LCLLKLMGEK GCTVTELSDF LQAMEHTEV LQL

UniProtKB: Mucosa-associated lymphoid tissue lymphoma translocation protein 1

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Experimental details

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Structure determination

Methodcryo EM
Processinghelical reconstruction
Aggregation statefilament

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Sample preparation

Concentration1 mg/mL
BufferpH: 7.5
GridModel: Quantifoil R1.2/1.3 / Material: COPPER
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeFEI TECNAI ARCTICA
Image recordingFilm or detector model: FEI FALCON III (4k x 4k) / Detector mode: INTEGRATING / Average electron dose: 99.6 e/Å2
Electron beamAcceleration voltage: 200 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD
Experimental equipment
Model: Talos Arctica / Image courtesy: FEI Company

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Image processing

Final reconstructionApplied symmetry - Helical parameters - Δz: 5.082 Å
Applied symmetry - Helical parameters - Δ&Phi: -100.8 °
Applied symmetry - Helical parameters - Axial symmetry: C1 (asymmetric)
Resolution.type: BY AUTHOR / Resolution: 4.9 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: SPRING (ver. 0.86) / Number images used: 9600
Segment selectionNumber selected: 25776 / Software - Name: SPRING (ver. 0.86)
Startup modelType of model: OTHER
Final angle assignmentType: NOT APPLICABLE
FSC plot (resolution estimation)

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