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TitleStructural basis for flagellin-induced NAIP5 activation.
Journal, issue, pagesSci Adv, Vol. 9, Issue 49, Page eadi8539, Year 2023
Publish dateDec 8, 2023
AuthorsBhaskar Paidimuddala / Jianhao Cao / Liman Zhang /
PubMed AbstractThe NAIP (NLR family apoptosis inhibitory protein)/NLRC4 (NLR family CARD containing protein 4) inflammasome senses Gram-negative bacterial ligand. In the ligand-bound state, the winged helix domain ...The NAIP (NLR family apoptosis inhibitory protein)/NLRC4 (NLR family CARD containing protein 4) inflammasome senses Gram-negative bacterial ligand. In the ligand-bound state, the winged helix domain of NAIP forms a steric clash with NLRC4 to open it up. However, how ligand binding activates NAIP is less clear. Here, we investigated the dynamics of the ligand-binding region of inactive NAIP5 and solved the cryo-EM structure of NAIP5 in complex with its specific ligand, FliC from flagellin, at 2.9-Å resolution. The structure revealed a "trap and lock" mechanism in FliC recognition, whereby FliC-D0 is first trapped by the hydrophobic pocket of NAIP5, then locked in the binding site by ID (insertion domain) and C-terminal tail of NAIP5. The FliC-D0 domain further inserts into ID to stabilize the complex. According to this mechanism, FliC triggers the conformational change of NAIP5 by bringing multiple flexible domains together.
External linksSci Adv / PubMed:38055825 / PubMed Central
MethodsEM (single particle)
Resolution2.93 Å
Structure data

29296

8fml

EMDB-29296, PDB-8fml:
Cryo-EM structure of NLR family apoptosis inhibitory protein 5 (NAIP5) in complex with a full-length flagellin (FliC) ligand
Method: EM (single particle) / Resolution: 2.93 Å

Source
  • mus musculus (house mouse)
  • salmonella enterica subsp. enterica serovar typhimurium str. lt2 (bacteria)
KeywordsIMMUNE SYSTEM / Inflammasome / Innate immunity / Bacterial ligand / host-pathogen interaction / Protein complex

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