6CIJ
Cryo-EM structure of mouse RAG1/2 HFC complex containing partial HMGB1 linker(3.9 A)
Summary for 6CIJ
| Entry DOI | 10.2210/pdb6cij/pdb |
| EMDB information | 7480 |
| Descriptor | V(D)J recombination-activating protein 1, ZINC ION, CALCIUM ION, ... (11 entities in total) |
| Functional Keywords | v(d)j recombination, rag1/2, rss, immunity, recombination, recombination-dna complex, recombination/dna |
| Biological source | Mus musculus (Mouse) More |
| Total number of polymer chains | 11 |
| Total formula weight | 378610.36 |
| Authors | Chen, X.,Kim, M.,Chuenchor, W.,Cui, Y.,Zhang, X.,Zhou, Z.H.,Gellert, M.,Yang, W. (deposition date: 2018-02-24, release date: 2018-04-25, Last modification date: 2024-03-13) |
| Primary citation | Kim, M.S.,Chuenchor, W.,Chen, X.,Cui, Y.,Zhang, X.,Zhou, Z.H.,Gellert, M.,Yang, W. Cracking the DNA Code for V(D)J Recombination. Mol. Cell, 70:358-370.e4, 2018 Cited by PubMed Abstract: To initiate V(D)J recombination for generating the adaptive immune response of vertebrates, RAG1/2 recombinase cleaves DNA at a pair of recombination signal sequences, the 12- and 23-RSS. We have determined crystal and cryo-EM structures of RAG1/2 with DNA in the pre-reaction and hairpin-forming complexes up to 2.75 Å resolution. Both protein and DNA exhibit structural plasticity and undergo dramatic conformational changes. Coding-flank DNAs extensively rotate, shift, and deform for nicking and hairpin formation. Two intertwined RAG1 subunits crisscross four times between the asymmetric pair of severely bent 12/23-RSS DNAs. Location-sensitive bending of 60° and 150° in 12- and 23-RSS spacers, respectively, must occur for RAG1/2 to capture the nonamers and pair the heptamers for symmetric double-strand breakage. DNA pairing is thus sequence-context dependent and structure specific, which partly explains the "beyond 12/23" restriction. Finally, catalysis in crystallo reveals the process of DNA hairpin formation and its stabilization by interleaved base stacking. PubMed: 29628308DOI: 10.1016/j.molcel.2018.03.008 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.9 Å) |
Structure validation
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