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- PDB-6bze: Cryo-EM structure of BCL10 CARD filament -

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Basic information

Entry
Database: PDB / ID: 6bze
TitleCryo-EM structure of BCL10 CARD filament
ComponentsB-cell lymphoma/leukemia 10
KeywordsSIGNALING PROTEIN / CARD / filament / signalosome / helical reconstruction
Function / homology
Function and homology information


positive regulation of lymphotoxin A production / polkadots / CBM complex / protein kinase B binding / antifungal innate immune response / 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 ...positive regulation of lymphotoxin A production / polkadots / CBM complex / protein kinase B binding / antifungal innate immune response / 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 / programmed cell death / positive regulation of extrinsic apoptotic signaling pathway / non-canonical NF-kappaB signal transduction / response to food / toll-like receptor signaling pathway / cytoplasmic microtubule / positive regulation of T cell receptor signaling pathway / : / general transcription initiation factor binding / immunoglobulin mediated immune response / immunological synapse / NF-kappaB binding / positive regulation of phosphorylation / cellular defense response / signaling adaptor activity / lipopolysaccharide-mediated signaling pathway / positive regulation of protein ubiquitination / neural tube closure / positive regulation of interleukin-8 production / Activation of NF-kappaB in B cells / protein homooligomerization / CLEC7A (Dectin-1) signaling / positive regulation of T cell activation / cellular response to mechanical stimulus / positive regulation of interleukin-6 production / FCERI mediated NF-kB activation / Downstream TCR signaling / E3 ubiquitin ligases ubiquitinate target proteins / T cell receptor signaling pathway / positive regulation of NF-kappaB transcription factor activity / protein-macromolecule adaptor activity / protease binding / cellular response to lipopolysaccharide / positive regulation of canonical NF-kappaB signal transduction / adaptive immune response / transcription coactivator activity / lysosome / positive regulation of apoptotic process / membrane raft / innate immune response / ubiquitin protein ligase binding / protein-containing complex binding / positive regulation of DNA-templated transcription / perinuclear region of cytoplasm / protein-containing complex / identical protein binding / nucleus / cytosol / cytoplasm
Similarity search - Function
B-cell lymphoma/leukemia 10/E10 / BCL10, CARD domain / CARD domain / CARD caspase recruitment domain profile. / Caspase recruitment domain / Death-like domain superfamily
Similarity search - Domain/homology
B-cell lymphoma/leukemia 10
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodELECTRON MICROSCOPY / helical reconstruction / cryo EM / Resolution: 4 Å
AuthorsDavid, L. / Li, Y. / Ma, J. / Garner, E. / Zhang, X. / Wu, H.
Funding support United States, 1items
OrganizationGrant numberCountry
National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)R01AI089882 United States
CitationJournal: Proc Natl Acad Sci U S A / Year: 2018
Title: Assembly mechanism of the CARMA1-BCL10-MALT1-TRAF6 signalosome.
Authors: Liron David / Yang Li / Jun Ma / Ethan Garner / Xinzheng Zhang / Hao Wu /
Abstract: The CARMA1-BCL10-MALT1 (CBM) signalosome is a central mediator of T cell receptor and B cell receptor-induced NF-κB signaling that regulates multiple lymphocyte functions. While caspase-recruitment ...The CARMA1-BCL10-MALT1 (CBM) signalosome is a central mediator of T cell receptor and B cell receptor-induced NF-κB signaling that regulates multiple lymphocyte functions. While caspase-recruitment domain (CARD) membrane-associated guanylate kinase (MAGUK) protein 1 (CARMA1) nucleates B cell lymphoma 10 (BCL10) filament formation through interactions between CARDs, mucosa-associated lymphoid tissue lymphoma translocation protein 1 (MALT1) is a paracaspase with structural similarity to caspases, which recruits TNF receptor-associated factor 6 (TRAF6) for K63-linked polyubiquitination. Here we present cryo-electron microscopy (cryo-EM) structure of the BCL10 CARD filament at 4.0-Å resolution. The structure redefines CARD-CARD interactions compared with the previous EM structure determined from a negatively stained sample. Surprisingly, time-lapse confocal imaging shows that BCL10 polymerizes in a unidirectional manner. CARMA1, the BCL10 nucleator, serves as a hub for formation of star-shaped filamentous networks of BCL10 and significantly decreases the lag period of BCL10 polymerization. Cooperative MALT1 interaction with BCL10 filaments observed under EM suggests immediate dimerization of MALT1 in the BCL10 filamentous scaffold. In addition, TRAF6 cooperatively decorates CBM filaments to form higher-order assemblies, likely resulting in all-or-none activation of the downstream pathway. Collectively, these data reveal biophysical mechanisms in the assembly of the CARMA1-BCL10-MALT1-TRAF6 complex for signal transduction.
History
DepositionDec 23, 2017Deposition site: RCSB / Processing site: RCSB
Revision 1.0Feb 14, 2018Provider: repository / Type: Initial release
Revision 1.1Feb 28, 2018Group: Database references / Category: citation
Item: _citation.journal_volume / _citation.page_first / _citation.page_last
Revision 1.2Dec 18, 2019Group: Author supporting evidence / Category: pdbx_audit_support / Item: _pdbx_audit_support.funding_organization
Revision 1.3Mar 13, 2024Group: Data collection / Database references / Refinement description
Category: chem_comp_atom / chem_comp_bond ...chem_comp_atom / chem_comp_bond / database_2 / em_3d_fitting_list / pdbx_initial_refinement_model
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _em_3d_fitting_list.accession_code / _em_3d_fitting_list.initial_refinement_model_id / _em_3d_fitting_list.source_name / _em_3d_fitting_list.type

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Structure visualization

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Assembly

Deposited unit
A: B-cell lymphoma/leukemia 10
B: B-cell lymphoma/leukemia 10
C: B-cell lymphoma/leukemia 10
D: B-cell lymphoma/leukemia 10
E: B-cell lymphoma/leukemia 10
F: B-cell lymphoma/leukemia 10
G: B-cell lymphoma/leukemia 10
H: B-cell lymphoma/leukemia 10


Theoretical massNumber of molelcules
Total (without water)100,9178
Polymers100,9178
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
  • Evidence: microscopy, gel filtration
TypeNameSymmetry operationNumber
identity operation1_5551
Buried area11000 Å2
ΔGint2 kcal/mol
Surface area45870 Å2

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Components

#1: Protein
B-cell lymphoma/leukemia 10 / B-cell CLL/lymphoma 10 / Bcl-10 / CARD-containing molecule enhancing NF-kappa-B / CARD-like ...B-cell CLL/lymphoma 10 / Bcl-10 / CARD-containing molecule enhancing NF-kappa-B / CARD-like apoptotic protein / hCLAP / CED-3/ICH-1 prodomain homologous E10-like regulator / CIPER / Cellular homolog of vCARMEN / cCARMEN / Cellular-E10 / c-E10 / Mammalian CARD-containing adapter molecule E10 / mE10


Mass: 12614.566 Da / Num. of mol.: 8
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Homo sapiens (human) / Gene: BCL10, CIPER, CLAP / Production host: Escherichia coli (E. coli) / References: UniProt: O95999

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Experimental details

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Experiment

ExperimentMethod: ELECTRON MICROSCOPY
EM experimentAggregation state: FILAMENT / 3D reconstruction method: helical reconstruction

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Sample preparation

ComponentName: BCL10 CARD / Type: COMPLEX / Entity ID: all / Source: RECOMBINANT
Molecular weightExperimental value: NO
Source (natural)Organism: Homo sapiens (human)
Source (recombinant)Organism: Escherichia coli (E. coli)
Buffer solutionpH: 7.5
Buffer component
IDConc.NameFormulaBuffer-ID
120 mMTrisC4H11NO31
2150 mMSodium ChlorideNaCl1
31 mMTCEPC9H15O6P1
SpecimenEmbedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
Specimen supportGrid material: COPPER / Grid mesh size: 400 divisions/in. / Grid type: C-flat-1.2/1.3 4C
VitrificationInstrument: FEI VITROBOT MARK III / Cryogen name: ETHANE / Humidity: 100 % / Chamber temperature: 278 K / Details: 5 second blotting time with force 3

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Electron microscopy imaging

Experimental equipment
Model: Talos Arctica / Image courtesy: FEI Company
MicroscopyModel: FEI TECNAI ARCTICA
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 200 kV / Illumination mode: FLOOD BEAM
Electron lensMode: BRIGHT FIELD / Nominal defocus max: 6000 nm / Nominal defocus min: 1000 nm / Cs: 2.7 mm / Alignment procedure: COMA FREE
Image recordingElectron dose: 40 e/Å2 / Detector mode: SUPER-RESOLUTION / Film or detector model: DIRECT ELECTRON DE-16 (4k x 4k) / Num. of grids imaged: 1 / Num. of real images: 339

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Processing

EM software
IDNameCategoryDetails
1EMAN2particle selectionEMAN2 e2helixboxer was used to select filament segments
2Leginonimage acquisition
4RELIONCTF correctionCTFFIND4
7PHENIXmodel fitting
9PHENIXmodel refinementPhenix refine
10IHRSRinitial Euler assignment
12RELIONclassification
13PHENIX3D reconstructionphenix refine
CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
Helical symmertyAngular rotation/subunit: -100.8 ° / Axial rise/subunit: 5 Å / Axial symmetry: C1
Particle selectionNum. of particles selected: 103873
3D reconstructionResolution: 4 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 39992 / Symmetry type: HELICAL
Atomic model buildingProtocol: RIGID BODY FIT
Atomic model buildingPDB-ID: 2MB9

2mb9


Pdb chain-ID: A / Accession code: 2MB9 / Pdb chain residue range: 10-115 / Source name: PDB / Type: experimental model

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