9IU8
Cryo-EM structure of the large serine recombinase Bxb1 in complex with attP and attB (GT/TT CDN) in the pre-strand exchange state (attP-L)
Summary for 9IU8
| Entry DOI | 10.2210/pdb9iu8/pdb |
| EMDB information | 60893 |
| Descriptor | Integrase, attP, ZINC ION, ... (4 entities in total) |
| Functional Keywords | large serine recombinase, dna binding protein |
| Biological source | Mycobacterium phage Bxb1 More |
| Total number of polymer chains | 3 |
| Total formula weight | 88548.87 |
| Authors | Soma, T.,Hiraizumi, M.,Yamashita, K.,Nishimasu, H. (deposition date: 2024-07-20, release date: 2026-03-04, Last modification date: 2026-06-24) |
| Primary citation | Soma, T.,Hiraizumi, M.,Fell, C.W.,Tagliaferri, D.,Lequyer, J.,Okazaki, S.,Isayama, Y.,Kato, K.,Sapkota, S.,Ramani, H.,Arya, B.,Schmitt-Ulms, C.,Yamashita, K.,Gootenberg, J.S.,Abudayyeh, O.O.,Nishimasu, H. Structure and engineering of the large serine recombinase Bxb1 for gene integration. Mol.Cell, 2026 Cited by PubMed Abstract: The large serine recombinase Bxb1 catalyzes recombination between DNA molecules containing compatible attP and attB sequences, offering broad applications in genome engineering and gene therapies. Here, we present cryo-electron microscopy structures of the Bxb1-attP-attB synaptic complex in four distinct functional states during its recombination cycle. Notably, the Bxb1 complex structures in the pre-, mid-, and post-strand-exchange states explain how the attP- and attB-bound Bxb1 dimers are assembled into a tetrameric synaptic complex and how an approximately 180° rotation occurs between the left and right dimers after DNA cleavage, thereby enabling DNA strand exchange and religation. Furthermore, we engineered Bxb1 variants with altered DNA preferences and enhanced recombination activity, which improved programmable gene integration in human cells. Overall, our findings advance the mechanistic understanding of large serine recombinases and provide a structural framework for future engineering of Bxb1-mediated genome integration technologies. PubMed: 42259299DOI: 10.1016/j.molcel.2026.05.018 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.21 Å) |
Structure validation
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