8VCT
CyoEM structure of the TnsC(1-503)-TnsD(1-318)-DNA complex in a 6:2:1 stoichiometry from E. coli Tn7 bound to ATPgS and ADP
Summary for 8VCT
| Entry DOI | 10.2210/pdb8vct/pdb |
| EMDB information | 43140 |
| Descriptor | Transposon Tn7 transposition protein TnsC, Transposon Tn7 transposition protein TnsD, DNA (50-MER), ... (8 entities in total) |
| Functional Keywords | transposon, aaa+ atpase, oligomer, complex, dna-binding protein dna complex, dna binding protein, dna binding protein-dna complex, dna binding protein/dna |
| Biological source | Escherichia coli More |
| Total number of polymer chains | 10 |
| Total formula weight | 463023.29 |
| Authors | |
| Primary citation | Shen, Y.,Krishnan, S.S.,Petassi, M.T.,Hancock, M.A.,Peters, J.E.,Guarne, A. Assembly of the Tn7 targeting complex by a regulated stepwise process. Mol.Cell, 84:2368-2381.e6, 2024 Cited by PubMed Abstract: The Tn7 family of transposons is notable for its highly regulated integration mechanisms, including programmable RNA-guided transposition. The targeting pathways rely on dedicated target selection proteins from the TniQ family and the AAA+ adaptor TnsC to recruit and activate the transposase at specific target sites. Here, we report the cryoelectron microscopy (cryo-EM) structures of TnsC bound to the TniQ domain of TnsD from prototypical Tn7 and unveil key regulatory steps stemming from unique behaviors of ATP- versus ADP-bound TnsC. We show that TnsD recruits ADP-bound dimers of TnsC and acts as an exchange factor to release one protomer with exchange to ATP. This loading process explains how TnsC assembles a heptameric ring unidirectionally from the target site. This unique loading process results in functionally distinct TnsC protomers within the ring, providing a checkpoint for target immunity and explaining how insertions at programmed sites precisely occur in a specific orientation across Tn7 elements. PubMed: 38834067DOI: 10.1016/j.molcel.2024.05.012 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.83 Å) |
Structure validation
Download full validation report
