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9Q1F

Choanoflagellate Salpingoeca macrocollata STING

Summary for 9Q1F
Entry DOI10.2210/pdb9q1f/pdb
DescriptorEndolysin,Stimulator of interferon genes, cGAMP (3 entities in total)
Functional Keywordsinnate immunity, cyclic dinucleotide signaling, stimulator of interferon genes, cgas-sting, immune system
Biological sourceSalpingoeca macrocollata
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Total number of polymer chains2
Total formula weight84996.02
Authors
Toyoda, H.C.,Li, Y.,Kranzusch, P.J. (deposition date: 2025-08-13, release date: 2025-10-01)
Primary citationLi, Y.,Toyoda, H.C.,Fernandez, S.G.,Tiwari, B.,McNairy, C.,Woznica, A.,Kranzusch, P.J.
A choanoflagellate cGLR-STING pathway reveals evolutionary links between bacterial and animal immunity.
Biorxiv, 2025
Cited by
PubMed Abstract: Animal innate immunity evolved from ancient pathways in bacterial anti-phage defense. How bacterial immune components were first acquired and adapted within eukaryotic cells remains poorly understood. Here we identify a complete cGLR-STING signaling axis in choanoflagellates, the closest living relatives of animals, that exhibits a mosaic of features from both bacterial and animal immunity. Comparative genomics reveals choanoflagellate and genes organized in operon-like arrangements reminiscent of bacterial defense loci. Reconstitution of choanoflagellate cGLR-STING signaling demonstrates that activation occurs through the conserved nucleotide immune signal 2'3'-cGAMP. Structural analysis of a choanoflagellate STING-2'3'-cGAMP complex explains how retention of bacterial-like features in early eukaryotic proteins shapes ligand specificity and receptor activation. We analyze and evolution in unicellular eukaryotes and identify further STING homologs in choanoflagellates and fungi that support additional independent acquisition events. Our results reveal molecular fossils that bridge bacterial and animal immunity and illuminate early eukaryotic immune system evolution.
PubMed: 40950183
DOI: 10.1101/2025.09.04.674280
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.65 Å)
Structure validation

242500

数据于2025-10-01公开中

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