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- PDB-1pn5: NMR structure of the NALP1 Pyrin domain (PYD) -

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Basic information

Entry
Database: PDB / ID: 1pn5
TitleNMR structure of the NALP1 Pyrin domain (PYD)
ComponentsNACHT-, LRR- and PYD-containing protein 2
KeywordsAPOPTOSIS / 5 ALPHA-HELIX BUNDLE
Function / homology
Function and homology information


NLRP1 inflammasome complex assembly / cysteine-type endopeptidase activator activity / NLRP1 inflammasome complex / inflammasome complex / self proteolysis / antiviral innate immune response / pattern recognition receptor signaling pathway / The NLRP1 inflammasome / Hydrolases; Acting on peptide bonds (peptidases) / pyroptosis ...NLRP1 inflammasome complex assembly / cysteine-type endopeptidase activator activity / NLRP1 inflammasome complex / inflammasome complex / self proteolysis / antiviral innate immune response / pattern recognition receptor signaling pathway / The NLRP1 inflammasome / Hydrolases; Acting on peptide bonds (peptidases) / pyroptosis / cysteine-type endopeptidase activator activity involved in apoptotic process / IgG binding / Hydrolases; Acting on acid anhydrides; Acting on acid anhydrides to facilitate cellular and subcellular movement / response to muramyl dipeptide / positive regulation of interleukin-1 beta production / protein homooligomerization / positive regulation of inflammatory response / activation of cysteine-type endopeptidase activity involved in apoptotic process / protein self-association / neuron apoptotic process / double-stranded RNA binding / regulation of inflammatory response / double-stranded DNA binding / defense response to virus / peptidase activity / endopeptidase activity / regulation of apoptotic process / inflammatory response / defense response to bacterium / protein domain specific binding / apoptotic process / nucleolus / ATP hydrolysis activity / enzyme binding / extracellular region / nucleoplasm / ATP binding / nucleus / cytosol / cytoplasm
Similarity search - Function
FIIND domain profile. / FIIND domain / Function to find / CARD8/ASC/NALP1, CARD domain / 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-NTPase domain profile. ...FIIND domain profile. / FIIND domain / Function to find / CARD8/ASC/NALP1, CARD domain / 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-NTPase domain profile. / NACHT domain / DAPIN domain / DAPIN domain profile. / PAAD/DAPIN/Pyrin domain / PAAD/DAPIN/Pyrin domain / B domain / IgG-binding B / Death Domain, Fas / Death Domain, Fas / M protein-type anchor domain / GA-like domain / GA-like domain / Leucine Rich repeat / Immunoglobulin/albumin-binding domain superfamily / CARD caspase recruitment domain profile. / CARD domain / Caspase recruitment domain / YSIRK Gram-positive signal peptide / LPXTG cell wall anchor motif / Gram-positive cocci surface proteins LPxTG motif profile. / LPXTG cell wall anchor domain / Leucine-rich repeat profile. / Death-like domain superfamily / Leucine-rich repeat / Leucine-rich repeat domain superfamily / P-loop containing nucleoside triphosphate hydrolase / Orthogonal Bundle / Mainly Alpha
Similarity search - Domain/homology
Immunoglobulin G-binding protein G / NACHT, LRR and PYD domains-containing protein 1
Similarity search - Component
Biological speciesHomo sapiens (human)
MethodSOLUTION NMR / torsion angle dynamics
AuthorsHiller, S. / Kohl, A. / Fiorito, F. / Herrmann, T. / Wider, G. / Tschopp, J. / Grutter, M.G. / Wuthrich, K.
CitationJournal: Structure / Year: 2003
Title: NMR structure of the apoptosis- and inflammation-related NALP1 pyrin domain
Authors: Hiller, S. / Kohl, A. / Fiorito, F. / Herrmann, T. / Wider, G. / Tschopp, J. / Grutter, M.G. / Wuthrich, K.
History
DepositionJun 12, 2003Deposition site: RCSB / Processing site: RCSB
Revision 1.0Oct 7, 2003Provider: repository / Type: Initial release
Revision 1.1Apr 29, 2008Group: Version format compliance
Revision 1.2Jul 13, 2011Group: Version format compliance
Revision 1.3Oct 27, 2021Group: Data collection / Database references / Derived calculations
Category: database_2 / pdbx_nmr_software ...database_2 / pdbx_nmr_software / pdbx_struct_assembly / pdbx_struct_oper_list / struct_ref_seq_dif
Item: _database_2.pdbx_DOI / _database_2.pdbx_database_accession ..._database_2.pdbx_DOI / _database_2.pdbx_database_accession / _pdbx_nmr_software.name / _struct_ref_seq_dif.details
Remark 999SEQUENCE Residues 1-58 are missing from the coordinates because they were not included in the model. ...SEQUENCE Residues 1-58 are missing from the coordinates because they were not included in the model. Residues 57 and 58 are independent linking residues, which have been inserted to provide distance and flexibiltiy in this two-domain fusion protein.
Remark 650HELIX Determination method: author

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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
A: NACHT-, LRR- and PYD-containing protein 2


Theoretical massNumber of molelcules
Total (without water)17,6811
Polymers17,6811
Non-polymers00
Water0
1


  • Idetical with deposited unit
  • defined by author
TypeNameSymmetry operationNumber
identity operation1_5551
NMR ensembles
DataCriteria
Number of conformers (submitted / calculated)20 / 100target function
RepresentativeModel #17aesthetic reasons

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Components

#1: Protein NACHT-, LRR- and PYD-containing protein 2 / Death effector filament-forming ced-4-like apoptosis protein / Nucleotide-binding domain and ...Death effector filament-forming ced-4-like apoptosis protein / Nucleotide-binding domain and caspase recruitment domain / Caspase recruitment domain protein 7


Mass: 17680.607 Da / Num. of mol.: 1 / Fragment: Pyrin domain (PYD)
Source method: isolated from a genetically manipulated source
Details: Residues 1-56 correspond to the fused Immunoglobulin G binding protein G (SWS P06654, residues 228-282)
Source: (gene. exp.) Homo sapiens (human) / Gene: NALP1 / Plasmid: pET20b+ / Production host: Escherichia coli (E. coli) / Strain (production host): BL21(DE3)pLysS / References: UniProt: P06654, UniProt: Q9C000

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Experimental details

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Experiment

ExperimentMethod: SOLUTION NMR
NMR experiment
Conditions-IDExperiment-IDSolution-IDType
1113D 15N-separated NOESY
1213D 13C-separated NOESY
NMR detailsText: Protein was expressed as a fusion protein with G B1 to enhance solubility (Zhou et al., J. Biomol. NMR 20, 11-14)

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Sample preparation

DetailsContents: 1mM NALP1 PYD U-15N,13C; 50mM Na / PO4 - Buffer; 50mM NaCl; 1mM CHAPS; 20mM DTT (D10); 0.02% NaN3; 0.1mM EDTA; protease inhibitor cocktail (Complete, Roche); 95% H2O, 5% D2O
Solvent system: 95% H2O/5% D2O
Sample conditionspH: 6.5 / Pressure: 1 atm / Temperature: 293 K
Crystal grow
*PLUS
Method: other / Details: NMR

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NMR measurement

RadiationProtocol: SINGLE WAVELENGTH / Monochromatic (M) / Laue (L): M
Radiation wavelengthRelative weight: 1
NMR spectrometer
TypeManufacturerModelField strength (MHz)Spectrometer-ID
Bruker DRXBrukerDRX7501
Bruker DRXBrukerDRX6002

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Processing

NMR software
NameDeveloperClassification
XwinNMRBrukercollection
DYANAGuentertstructure solution
CANDIDHerrmannstructure solution
ATNOSHerrmannstructure solution
CARAKellerdata analysis
ATNOSHerrmannrefinement
RefinementMethod: torsion angle dynamics / Software ordinal: 1
NMR representativeSelection criteria: aesthetic reasons
NMR ensembleConformer selection criteria: target function / Conformers calculated total number: 100 / Conformers submitted total number: 20

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