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TitleStructural basis for recognition of N-formyl peptides as pathogen-associated molecular patterns.
Journal, issue, pagesNat Commun, Vol. 13, Issue 1, Page 5232, Year 2022
Publish dateSep 5, 2022
AuthorsGeng Chen / Xiankun Wang / Qiwen Liao / Yunjun Ge / Haizhan Jiao / Qiang Chen / Yezhou Liu / Wenping Lyu / Lizhe Zhu / Gydo C P van Zundert / Michael J Robertson / Georgios Skiniotis / Yang Du / Hongli Hu / Richard D Ye /
PubMed AbstractThe formyl peptide receptor 1 (FPR1) is primarily responsible for detection of short peptides bearing N-formylated methionine (fMet) that are characteristic of protein synthesis in bacteria and ...The formyl peptide receptor 1 (FPR1) is primarily responsible for detection of short peptides bearing N-formylated methionine (fMet) that are characteristic of protein synthesis in bacteria and mitochondria. As a result, FPR1 is critical to phagocyte migration and activation in bacterial infection, tissue injury and inflammation. How FPR1 distinguishes between formyl peptides and non-formyl peptides remains elusive. Here we report cryo-EM structures of human FPR1-Gi protein complex bound to S. aureus-derived peptide fMet-Ile-Phe-Leu (fMIFL) and E. coli-derived peptide fMet-Leu-Phe (fMLF). Both structures of FPR1 adopt an active conformation and exhibit a binding pocket containing the R201XXXR205 (RGIIR) motif for formyl group interaction and receptor activation. This motif works together with D106 for hydrogen bond formation with the N-formyl group and with fMet, a model supported by MD simulation and functional assays of mutant receptors with key residues for recognition substituted by alanine. The cryo-EM model of agonist-bound FPR1 provides a structural basis for recognition of bacteria-derived chemotactic peptides with potential applications in developing FPR1-targeting agents.
External linksNat Commun / PubMed:36064945 / PubMed Central
MethodsEM (single particle)
Resolution2.8 - 2.9 Å
Structure data

31323

7euo

EMDB-31323, PDB-7euo:
The structure of formyl peptide receptor 1 in complex with Gi and peptide agonist fMLF
Method: EM (single particle) / Resolution: 2.9 Å

31962

7vfx

EMDB-31962, PDB-7vfx:
The structure of Formyl Peptide Receptor 1 in complex with Gi and peptide agonist fMIFL
Method: EM (single particle) / Resolution: 2.8 Å

Chemicals

ChemComp-CLR:
CHOLESTEROL / Cholesterol

ChemComp-PLM:
PALMITIC ACID / Palmitic acid

Source
  • homo sapiens (human)
  • mus musculus (house mouse)
  • escherichia coli (E. coli)
  • staphylococcus aureus (bacteria)
KeywordsSIGNALING PROTEIN/IMMUNE SYSTEM / Formyl peptide receptor 1 / Gi complex / SIGNALING PROTEIN / SIGNALING PROTEIN-IMMUNE SYSTEM complex / SIGNALING PROTEIN/PROTEIN BINDING / SIGNALING PROTEIN-PROTEIN BINDING complex

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