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9MTY

Structure of TIGR-TasR in complex with tigRNA and target DNA after DNA cleavage

Summary for 9MTY
Entry DOI10.2210/pdb9mty/pdb
EMDB information48616
DescriptorTransposase IS116/IS110/IS902 C-terminal domain-containing protein, tigRNA, Target DNA, spacer A targeted strand, 5' of cut, ... (7 entities in total)
Functional Keywordsnuclease, rna-guided, nop domain, dna-binding protein, dna-rna hybrid, dna binding protein-rna-dna complex, dna binding protein/rna/dna
Biological sourceThermoproteota archaeon
More
Total number of polymer chains7
Total formula weight125026.63
Authors
Wilkinson, M.E.,Zhang, F. (deposition date: 2025-01-12, release date: 2025-03-05, Last modification date: 2025-05-14)
Primary citationFaure, 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: 40014690
DOI: 10.1126/science.adv9789
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.05 Å)
Structure validation

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