7MBW
Crystal structure of TnsC(1-503)A225V
Summary for 7MBW
| Entry DOI | 10.2210/pdb7mbw/pdb |
| Descriptor | Transposon Tn7 transposition protein TnsC, ADENOSINE-5'-DIPHOSPHATE, MAGNESIUM ION, ... (4 entities in total) |
| Functional Keywords | aaa+ atpase, transposition, dna binding, dna binding protein |
| Biological source | Escherichia coli |
| Total number of polymer chains | 4 |
| Total formula weight | 241444.92 |
| Authors | Shen, Y.,Guarne, A. (deposition date: 2021-04-01, release date: 2022-02-23, Last modification date: 2024-11-06) |
| Primary citation | Shen, Y.,Gomez-Blanco, J.,Petassi, M.T.,Peters, J.E.,Ortega, J.,Guarne, A. Structural basis for DNA targeting by the Tn7 transposon. Nat.Struct.Mol.Biol., 29:143-151, 2022 Cited by PubMed Abstract: Tn7 transposable elements are unique for their highly specific, and sometimes programmable, target-site selection mechanisms and precise insertions. All the elements in the Tn7 family utilize an AAA+ adaptor (TnsC) to coordinate target-site selection with transpososome assembly and to prevent insertions at sites already containing a Tn7 element. Owing to its multiple functions, TnsC is considered the linchpin in the Tn7 element. Here we present the high-resolution cryo-EM structure of TnsC bound to DNA using a gain-of-function variant of the protein and a DNA substrate that together recapitulate the recruitment to a specific DNA target site. TnsC forms an asymmetric ring on target DNA that segregates target-site selection and interaction with the paired-end complex to opposite faces of the ring. Unlike most AAA+ ATPases, TnsC uses a DNA distortion to find the target site but does not remodel DNA to activate transposition. By recognizing pre-distorted substrates, TnsC creates a built-in regulatory mechanism where ATP hydrolysis abolishes ring formation proximal to an existing element. This work unveils how Tn7 and Tn7-like elements determine the strict spacing between the target and integration sites. PubMed: 35173349DOI: 10.1038/s41594-022-00724-8 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.2 Å) |
Structure validation
Download full validation report
