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- PDB-7crw: Cryo-EM structure of rNLRP1-rDPP9 complex -

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Basic information

Entry
Database: PDB / ID: 7crw
TitleCryo-EM structure of rNLRP1-rDPP9 complex
Components
  • Dipeptidyl peptidase 9
  • NLR family protein 1
KeywordsIMMUNE SYSTEM
Function / homology
Function and homology information


negative regulation of cellular defense response / NLRP1 inflammasome complex assembly / NLRP1 inflammasome complex / programmed necrotic cell death / NLRP3 inflammasome complex / self proteolysis / positive regulation of pyroptotic inflammatory response / dipeptidyl-peptidase IV / cysteine-type endopeptidase activator activity / dipeptidyl-peptidase activity ...negative regulation of cellular defense response / NLRP1 inflammasome complex assembly / NLRP1 inflammasome complex / programmed necrotic cell death / NLRP3 inflammasome complex / self proteolysis / positive regulation of pyroptotic inflammatory response / dipeptidyl-peptidase IV / cysteine-type endopeptidase activator activity / dipeptidyl-peptidase activity / Hydrolases; Acting on peptide bonds (peptidases) / negative regulation of programmed cell death / cellular response to UV-B / pattern recognition receptor activity / pyroptotic inflammatory response / cell leading edge / response to muramyl dipeptide / aminopeptidase activity / signaling adaptor activity / antiviral innate immune response / serine-type peptidase activity / activation of innate immune response / intrinsic apoptotic signaling pathway / positive regulation of interleukin-1 beta production / molecular condensate scaffold activity / protein homooligomerization / positive regulation of inflammatory response / peptidase activity / double-stranded RNA binding / double-stranded DNA binding / regulation of inflammatory response / scaffold protein binding / neuron apoptotic process / regulation of apoptotic process / defense response to virus / microtubule / defense response to bacterium / inflammatory response / protein domain specific binding / neuronal cell body / enzyme binding / signal transduction / protein-containing complex / ATP hydrolysis activity / proteolysis / ATP binding / identical protein binding / nucleus / cytosol
Similarity search - Function
FIIND domain / Function to find / UPA-FIIND domain / FIIND domain profile. / CARD8/ASC/NALP1, CARD domain / Dipeptidyl peptidase 8 /9 ,N-terminal / Dipeptidyl peptidase 8 and 9 N-terminal / : / NACHT, LRR and PYD domains-containing protein, helical domain HD2 / NLRC4 helical domain HD2 ...FIIND domain / Function to find / UPA-FIIND domain / FIIND domain profile. / CARD8/ASC/NALP1, CARD domain / Dipeptidyl peptidase 8 /9 ,N-terminal / Dipeptidyl peptidase 8 and 9 N-terminal / : / NACHT, LRR and PYD domains-containing protein, helical domain HD2 / NLRC4 helical domain HD2 / NOD2, winged helix domain / NOD2 winged helix domain / NACHT nucleoside triphosphatase / NACHT domain / NACHT-NTPase domain profile. / Dipeptidylpeptidase IV, N-terminal domain / Leucine rich repeat, ribonuclease inhibitor type / : / Dipeptidylpeptidase IV, N-terminal domain / Dipeptidyl peptidase IV (DPP IV) N-terminal region / 8 Propeller / Methanol Dehydrogenase; Chain A / Leucine Rich repeat / CARD domain / CARD caspase recruitment domain profile. / Caspase recruitment domain / Peptidase S9, prolyl oligopeptidase, catalytic domain / Prolyl oligopeptidase family / Death-like domain superfamily / Leucine-rich repeat / Leucine-rich repeat domain superfamily / Alpha/Beta hydrolase fold, catalytic domain / Alpha/Beta hydrolase fold / Rossmann fold / P-loop containing nucleoside triphosphate hydrolase / 3-Layer(aba) Sandwich / Mainly Beta / Alpha Beta
Similarity search - Domain/homology
NACHT, LRR and PYD domains-containing protein 1 allele 2 / dipeptidyl-peptidase IV
Similarity search - Component
Biological speciesRattus norvegicus (Norway rat)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.18 Å
AuthorsHuang, M.H. / Zhang, X.X. / Wang, J. / Chai, J.J.
Funding support China, 1items
OrganizationGrant numberCountry
National Natural Science Foundation of China (NSFC)31421001 to J.C. China
CitationJournal: Nature / Year: 2021
Title: Structural and biochemical mechanisms of NLRP1 inhibition by DPP9.
Authors: Menghang Huang / Xiaoxiao Zhang / Gee Ann Toh / Qin Gong / Jia Wang / Zhifu Han / Bin Wu / Franklin Zhong / Jijie Chai /
Abstract: Nucleotide-binding domain, leucine-rich repeat receptors (NLRs) mediate innate immunity by forming inflammasomes. Activation of the NLR protein NLRP1 requires autocleavage within its function-to-find ...Nucleotide-binding domain, leucine-rich repeat receptors (NLRs) mediate innate immunity by forming inflammasomes. Activation of the NLR protein NLRP1 requires autocleavage within its function-to-find domain (FIIND). In resting cells, the dipeptidyl peptidases DPP8 and DPP9 interact with the FIIND of NLRP1 and suppress spontaneous NLRP1 activation; however, the mechanisms through which this occurs remain unknown. Here we present structural and biochemical evidence that full-length rat NLRP1 (rNLRP1) and rat DPP9 (rDPP9) form a 2:1 complex that contains an autoinhibited rNLRP1 molecule and an active UPA-CARD fragment of rNLRP1. The ZU5 domain is required not only for autoinhibition of rNLRP1 but also for assembly of the 2:1 complex. Formation of the complex prevents UPA-mediated higher-order oligomerization of UPA-CARD fragments and strengthens ZU5-mediated NLRP1 autoinhibition. Structure-guided biochemical and functional assays show that both NLRP1 binding and enzymatic activity are required for DPP9 to suppress NLRP1 in human cells. Together, our data reveal the mechanism of DPP9-mediated inhibition of NLRP1 and shed light on the activation of the NLRP1 inflammasome.
History
DepositionAug 14, 2020Deposition site: PDBJ / Processing site: PDBJ
Revision 1.0Mar 24, 2021Provider: repository / Type: Initial release
Revision 1.1Mar 31, 2021Group: Database references / Category: citation / citation_author
Item: _citation.pdbx_database_id_PubMed / _citation.title / _citation_author.name
Revision 1.2May 12, 2021Group: Database references / Category: citation
Item: _citation.journal_volume / _citation.page_first / _citation.page_last
Revision 1.3Mar 27, 2024Group: Data collection / Database references / Category: chem_comp_atom / chem_comp_bond / database_2
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession

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Structure visualization

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Assembly

Deposited unit
D: Dipeptidyl peptidase 9
A: NLR family protein 1
B: NLR family protein 1
C: Dipeptidyl peptidase 9


Theoretical massNumber of molelcules
Total (without water)473,5624
Polymers473,5624
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author
  • Evidence: gel filtration
TypeNameSymmetry operationNumber
identity operation1_5551

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Components

#1: Protein Dipeptidyl peptidase 9


Mass: 98203.273 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Rattus norvegicus (Norway rat) / Gene: Dpp9 / Production host: Spodoptera frugiperda (fall armyworm) / References: UniProt: M0R781
#2: Protein NLR family protein 1


Mass: 138577.859 Da / Num. of mol.: 2
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Rattus norvegicus (Norway rat) / Gene: Nlrp1 / Production host: Spodoptera frugiperda (fall armyworm) / References: UniProt: D9I2G3

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Experimental details

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Experiment

ExperimentMethod: ELECTRON MICROSCOPY
EM experimentAggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction

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Sample preparation

ComponentName: Complex of Nlrp1-FIIND with DPP9 dimer / Type: COMPLEX / Entity ID: all / Source: RECOMBINANT
Source (natural)Organism: Rattus norvegicus (Norway rat)
Source (recombinant)Organism: Spodoptera frugiperda (fall armyworm)
Buffer solutionpH: 8
SpecimenEmbedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
VitrificationCryogen name: ETHANE

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Electron microscopy imaging

Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company
MicroscopyModel: FEI TITAN KRIOS
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM
Electron lensMode: BRIGHT FIELD
Image recordingElectron dose: 50 e/Å2 / Film or detector model: GATAN K2 SUMMIT (4k x 4k)

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Processing

SoftwareName: PHENIX / Version: 1.15.1_3469: / Classification: refinement
CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
3D reconstructionResolution: 3.18 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 182116 / Symmetry type: POINT
Refine LS restraints
Refine-IDTypeDev idealNumber
ELECTRON MICROSCOPYf_bond_d0.00417116
ELECTRON MICROSCOPYf_angle_d0.56123244
ELECTRON MICROSCOPYf_dihedral_angle_d6.78410148
ELECTRON MICROSCOPYf_chiral_restr0.0442474
ELECTRON MICROSCOPYf_plane_restr0.0043008

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