8GLU
CryoEM structure of TnsC(1-503) bound to TnsD(1-318) from E.coli Tn7
Summary for 8GLU
| Entry DOI | 10.2210/pdb8glu/pdb |
| EMDB information | 40218 |
| Descriptor | Transposon Tn7 transposition protein TnsC, Transposon Tn7 transposition protein TnsD, ADENOSINE-5'-TRIPHOSPHATE, ... (6 entities in total) |
| Functional Keywords | transposon, aaa+ atpase, oligomer, complex, dna binding protein |
| Biological source | Escherichia coli More |
| Total number of polymer chains | 4 |
| Total formula weight | 216172.68 |
| 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 (3.57 Å) |
Structure validation
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