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TitleStructural and biochemical basis for induced self-propagation of NLRC4.
Journal, issue, pagesScience, Vol. 350, Issue 6259, Page 399-404, Year 2015
Publish dateOct 23, 2015
AuthorsZehan Hu / Qiang Zhou / Chenlu Zhang / Shilong Fan / Wei Cheng / Yue Zhao / Feng Shao / Hong-Wei Wang / Sen-Fang Sui / Jijie Chai /
PubMed AbstractResponding to stimuli, nucleotide-binding domain and leucine-rich repeat-containing proteins (NLRs) oligomerize into multiprotein complexes, termed inflammasomes, mediating innate immunity. ...Responding to stimuli, nucleotide-binding domain and leucine-rich repeat-containing proteins (NLRs) oligomerize into multiprotein complexes, termed inflammasomes, mediating innate immunity. Recognition of bacterial pathogens by NLR apoptosis inhibitory proteins (NAIPs) induces NLR family CARD domain-containing protein 4 (NLRC4) activation and formation of NAIP-NLRC4 inflammasomes. The wheel-like structure of a PrgJ-NAIP2-NLRC4 complex determined by cryogenic electron microscopy at 6.6 angstrom reveals that NLRC4 activation involves substantial structural reorganization that creates one oligomerization surface (catalytic surface). Once activated, NLRC4 uses this surface to catalyze the activation of an inactive NLRC4, self-propagating its active conformation to form the wheel-like architecture. NAIP proteins possess a catalytic surface matching the other oligomerization surface (receptor surface) of NLRC4 but not those of their own, ensuring that one NAIP is sufficient to initiate NLRC4 oligomerization.
External linksScience / PubMed:26449475
MethodsEM (single particle)
Resolution6.7 - 25.2 Å
Structure data

EMDB-3139:
Electron cryo-microscopy of PrgJ/NAIP2/full-length NLRC4 inflammasome with pseudo c12 symmetry
Method: EM (single particle) / Resolution: 10.1 Å

EMDB-3140:
Electron cryo-microscopy of PrgJ/NAIP2/full-length NLRC4 inflammasome with pseudo c11 symmetry
Method: EM (single particle) / Resolution: 8.1 Å

EMDB-3141:
Electron cryo-microscopy of PrgJ/NAIP2/CARD-truncated NLRC4 inflammasome with pseudo c11 symmetry
Method: EM (single particle) / Resolution: 6.7 Å

EMDB-3142:
Electron cryo-microscopy of PrgJ/NAIP2/CARD-truncated NLRC4 inflammasome with pseudo c10 symmetry
Method: EM (single particle) / Resolution: 6.7 Å

EMDB-3143:
Electron microscopy of flagellin/NAIP5/CARD-truncated NLRC4(R288A)
Method: EM (single particle) / Resolution: 25.2 Å

Source
  • Mus musculus (house mouse)
  • Salmonella enterica subsp. enterica serovar Typhimurium (bacteria)

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