Transposase for transposon Tn5 (TN5P)

Tn5 is derived from Escherichia coli, and the Tnp sequence is 476 amino acids in length. Tn5Tnp consists of three domains: the N-terminal, the catalytic domain and the C-terminal. The N-terminal contains 70 amino acids, which compose many A-helices and β-corners for ONA binding. The active center of Tnp is located in the middle 300 amino acids, which contains a "ribonuclease H-like motif" and a a/β/a folding structure mixed with β lamellar structure. The C-terminal consists entirely of a helix and is primarily responsible for protein-protein interactions. At the beginning of transposition, the two transTNPs recognize the OE sequence at both ends of the binding Tn5 transposon, forming the Tnp-OE complex, and then the two Tnp-OE complexes bind to each other, and the C ends of the two TNPS mediate the interaction and form a dimeric synaptic complex with the ability to cut DNA.