6OET
Cryo-EM structure of mouse RAG1/2 STC complex
Summary for 6OET
Entry DOI | 10.2210/pdb6oet/pdb |
Related | 6OEM 6OEN 6OEO 6OEP 6OEQ 6OER 6OES |
EMDB information | 20030 20031 20032 20033 20034 20035 20036 20037 |
Descriptor | V(D)J recombination-activating protein 1, V(D)J recombination-activating protein 2, DNA (50-MER), ... (9 entities in total) |
Functional Keywords | v(d)j recombination, dna transposition, rag, scid, recombination, recombination-dna complex, recombination/dna |
Biological source | Mus musculus (Mouse) More |
Total number of polymer chains | 10 |
Total formula weight | 422496.41 |
Authors | Chen, X.,Cui, Y.,Zhou, Z.H.,Yang, W.,Gellert, M. (deposition date: 2019-03-27, release date: 2020-01-22, Last modification date: 2025-05-21) |
Primary citation | Chen, X.,Cui, Y.,Wang, H.,Zhou, Z.H.,Gellert, M.,Yang, W. How mouse RAG recombinase avoids DNA transposition. Nat.Struct.Mol.Biol., 27:127-133, 2020 Cited by PubMed Abstract: The RAG1-RAG2 recombinase (RAG) cleaves DNA to initiate V(D)J recombination, but RAG also belongs to the RNH-type transposase family. To learn how RAG-catalyzed transposition is inhibited in developing lymphocytes, we determined the structure of a DNA-strand transfer complex of mouse RAG at 3.1-Å resolution. The target DNA is a T form (T for transpositional target), which contains two >80° kinks towards the minor groove, only 3 bp apart. RAG2, a late evolutionary addition in V(D)J recombination, appears to enforce the sharp kinks and additional inter-segment twisting in target DNA and thus attenuates unwanted transposition. In contrast to strand transfer complexes of genuine transposases, where severe kinks occur at the integration sites of target DNA and thus prevent the reverse reaction, the sharp kink with RAG is 1 bp away from the integration site. As a result, RAG efficiently catalyzes the disintegration reaction that restores the RSS (donor) and target DNA. PubMed: 32015553DOI: 10.1038/s41594-019-0366-z PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (3.4 Å) |
Structure validation
Download full validation report
