9MTY
Structure of TIGR-TasR in complex with tigRNA and target DNA after DNA cleavage
Summary for 9MTY
Entry DOI | 10.2210/pdb9mty/pdb |
EMDB information | 48616 |
Descriptor | Transposase IS116/IS110/IS902 C-terminal domain-containing protein, tigRNA, Target DNA, spacer A targeted strand, 5' of cut, ... (7 entities in total) |
Functional Keywords | nuclease, rna-guided, nop domain, dna-binding protein, dna-rna hybrid, dna binding protein-rna-dna complex, dna binding protein/rna/dna |
Biological source | Thermoproteota archaeon More |
Total number of polymer chains | 7 |
Total formula weight | 125026.63 |
Authors | Wilkinson, M.E.,Zhang, F. (deposition date: 2025-01-12, release date: 2025-03-05, Last modification date: 2025-05-14) |
Primary citation | Faure, G.,Saito, M.,Wilkinson, M.E.,Quinones-Olvera, N.,Xu, P.,Flam-Shepherd, D.,Kim, S.,Reddy, N.,Zhu, S.,Evgeniou, L.,Koonin, E.V.,Macrae, R.K.,Zhang, F. TIGR-Tas: A family of modular RNA-guided DNA-targeting systems in prokaryotes and their viruses. Science, 388:eadv9789-eadv9789, 2025 Cited by PubMed Abstract: RNA-guided systems provide remarkable versatility, enabling diverse biological functions. Through iterative structural and sequence homology-based mining starting with a guide RNA-interaction domain of Cas9, we identified a family of RNA-guided DNA-targeting proteins in phage and parasitic bacteria. Each system consists of a Tandem Interspaced Guide RNA (TIGR) array and a TIGR-associated (Tas) protein containing a Nop domain, sometimes fused to HNH (TasH) or RuvC (TasR) nuclease domains. We show that TIGR arrays are processed into 36-nt RNAs (tigRNAs) that direct sequence-specific DNA binding through a tandem-spacer targeting mechanism. TasR can be reprogrammed for precise DNA cleavage, including in human cells. The structure of TasR reveals striking similarities to box C/D snoRNPs and IS110 RNA-guided transposases, providing insights into the evolution of diverse RNA-guided systems. PubMed: 40014690DOI: 10.1126/science.adv9789 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (3.05 Å) |
Structure validation
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