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8IBW

Structure of R2 with 3'UTR and DNA in binding state

Summary for 8IBW
Entry DOI10.2210/pdb8ibw/pdb
EMDB information35347
DescriptorDNA (60-MER), Reverse transcriptase-like protein, 3'UTR, ... (5 entities in total)
Functional Keywordsr2 complex, rna binding protein/rna/dna, rna binding protein-rna-dna complex
Biological sourceBombyx mori (domestic silkworm)
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Total number of polymer chains4
Total formula weight176527.49
Authors
Deng, P.,Tan, S.,Wang, J.,Liu, J.J. (deposition date: 2023-02-10, release date: 2023-09-20)
Primary citationDeng, P.,Tan, S.Q.,Yang, Q.Y.,Fu, L.,Wu, Y.,Zhu, H.Z.,Sun, L.,Bao, Z.,Lin, Y.,Zhang, Q.C.,Wang, H.,Wang, J.,Liu, J.G.
Structural RNA components supervise the sequential DNA cleavage in R2 retrotransposon.
Cell, 186:2865-2879.e20, 2023
Cited by
PubMed Abstract: Retroelements are the widespread jumping elements considered as major drivers for genome evolution, which can also be repurposed as gene-editing tools. Here, we determine the cryo-EM structures of eukaryotic R2 retrotransposon with ribosomal DNA target and regulatory RNAs. Combined with biochemical and sequencing analysis, we reveal two essential DNA regions, Drr and Dcr, required for recognition and cleavage. The association of 3' regulatory RNA with R2 protein accelerates the first-strand cleavage, blocks the second-strand cleavage, and initiates the reverse transcription starting from the 3'-tail. Removing 3' regulatory RNA by reverse transcription allows the association of 5' regulatory RNA and initiates the second-strand cleavage. Taken together, our work explains the DNA recognition and RNA supervised sequential retrotransposition mechanisms by R2 machinery, providing insights into the retrotransposon and application reprogramming.
PubMed: 37301196
DOI: 10.1016/j.cell.2023.05.032
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.6 Å)
Structure validation

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