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9JFP

Structure of LaTranC complex bound to 6nt complementary DNA substrate

Summary for 9JFP
Entry DOI10.2210/pdb9jfp/pdb
EMDB information61435
DescriptorDNA (37-MER), RNA (195-MER), LaTranC, ... (4 entities in total)
Functional Keywordslatranc complexes, immune system/dna/rna, immune system-dna-rna complex
Biological sourceLawsonibacter sp.
More
Total number of polymer chains4
Total formula weight139682.12
Authors
Zhang, S.,Liu, J. (deposition date: 2024-09-05, release date: 2025-10-08, Last modification date: 2025-11-26)
Primary citationJin, S.,Zhu, Z.,Li, Y.,Zhang, S.,Liu, Y.,Li, D.,Li, Y.,Luo, Y.,Cheng, Z.,Zhao, K.T.,Gao, Q.,Yang, G.,Li, H.,Liang, R.,Zhang, R.,Qiu, J.L.,Zhang, Y.E.,Liu, J.G.,Gao, C.
Functional RNA splitting drove the evolutionary emergence of type V CRISPR-Cas systems from transposons.
Cell, 188:6283-6300.e22, 2025
Cited by
PubMed Abstract: Transposon-encoded TnpB nucleases gave rise to type V CRISPR-Cas12 effectors through multiple independent domestication events. These systems use different RNA molecules as guides for DNA targeting: transposon-derived right-end RNAs (reRNAs or omega RNAs) for TnpB and CRISPR RNAs for type V CRISPR-Cas systems. However, the molecular mechanisms bridging transposon activity and CRISPR immunity remain unclear. We identify TranCs (transposon-CRISPR intermediates) derived from distinct IS605- or IS607-TnpB lineages. TranCs utilize both CRISPR RNAs and reRNAs to direct DNA cleavage. The cryoelectron microscopy (cryo-EM) structure of LaTranC from Lawsonibacter sp. closely resembles that of the ISDra2 TnpB complex; however, unlike a single-molecule reRNA, the LaTranC guide RNA is functionally split into a tracrRNA and crRNA. An engineered RNA split of ISDra2 TnpB enabled activity with a CRISPR array. These findings indicate that functional RNA splitting was the primary molecular event driving the emergence of diverse type V CRISPR-Cas systems from transposons.
PubMed: 41027434
DOI: 10.1016/j.cell.2025.09.004
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (2.96 Å)
Structure validation

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