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TitleRecognition of phylogenetically diverse pathogens through enzymatically amplified recruitment of RNF213.
Journal, issue, pagesEMBO Rep, Vol. 25, Issue 11, Page 4979-5005, Year 2024
Publish dateOct 7, 2024
AuthorsAna Crespillo-Casado / Prathyush Pothukuchi / Katerina Naydenova / Matthew C J Yip / Janet M Young / Jerome Boulanger / Vimisha Dharamdasani / Ceara Harper / Pierre-Mehdi Hammoudi / Elsje G Otten / Keith Boyle / Mayuri Gogoi / Harmit S Malik / Felix Randow /
PubMed AbstractInnate immunity senses microbial ligands known as pathogen-associated molecular patterns (PAMPs). Except for nucleic acids, PAMPs are exceedingly taxa-specific, thus enabling pattern recognition ...Innate immunity senses microbial ligands known as pathogen-associated molecular patterns (PAMPs). Except for nucleic acids, PAMPs are exceedingly taxa-specific, thus enabling pattern recognition receptors to detect cognate pathogens while ignoring others. How the E3 ubiquitin ligase RNF213 can respond to phylogenetically distant pathogens, including Gram-negative Salmonella, Gram-positive Listeria, and eukaryotic Toxoplasma, remains unknown. Here we report that the evolutionary history of RNF213 is indicative of repeated adaptation to diverse pathogen target structures, especially in and around its newly identified CBM20 carbohydrate-binding domain, which we have resolved by cryo-EM. We find that RNF213 forms coats on phylogenetically distant pathogens. ATP hydrolysis by RNF213's dynein-like domain is essential for coat formation on all three pathogens studied as is RZ finger-mediated E3 ligase activity for bacteria. Coat formation is not diffusion-limited but instead relies on rate-limiting initiation events and subsequent cooperative incorporation of further RNF213 molecules. We conclude that RNF213 responds to evolutionarily distant pathogens through enzymatically amplified cooperative recruitment.
External linksEMBO Rep / PubMed:39375464 / PubMed Central
MethodsEM (single particle)
Resolution2.9 - 3.2 Å
Structure data

19653

8s24

EMDB-19653, PDB-8s24:
Structure of the E3 ubiquitin ligase RNF213, determined by cryoEM
Method: EM (single particle) / Resolution: 3.0 Å

EMDB-19654: Human RNF213 (consensus refinement without accounting for flexibility)
Method: EM (single particle) / Resolution: 3.0 Å

EMDB-19655: Human RNF213: focused refinement of ATPase domain
Method: EM (single particle) / Resolution: 2.9 Å

EMDB-19656: Human RNF213: focused refinement of stalk domain
Method: EM (single particle) / Resolution: 3.1 Å

EMDB-19657: Human RNF213: focused refinement of carbohydrate binding module (CBM) domain
Method: EM (single particle) / Resolution: 3.2 Å

EMDB-19658: Human RNF213: focused refinement of E3 ligase domain
Method: EM (single particle) / Resolution: 3.1 Å

EMDB-19659: Human RNF213: focused refinement of E3-RING domain
Method: EM (single particle) / Resolution: 3.1 Å

Chemicals

ChemComp-ATP:
ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying molecule*YM

ChemComp-MG:
Unknown entry

ChemComp-ZN:
Unknown entry

Source
  • homo sapiens (human)
KeywordsANTIMICROBIAL PROTEIN / E3 ubiquitin ligase / ATPase / carbohydrate-binding domain / RING domain / RZ domain

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