4dm0 | pdb_00004dm0
TN5 transposase: 20MER OUTSIDE END 2 MN complex
Structural highlights
Function[TN5P_ECOLX] Mediates transposition of transposon Tn5 by a 'cut and paste' mechanism. First, the monomeric transposase binds the 19 bp inverted DNA repeats flanking the transposon. Then, dimerization of the DNA-bound transposase creates a synaptic DNA complex. After nicking of the first DNA strand, excision of the transposon proceeds through a series of intermediates. The transposase then mediates the insertion of the transposon at a new site by strand transfer. The activity of the wild-type transposase is very low, and is further inhibited by dimerization with the transposase inhibitor (inh).[1] [2] [3] [4] [5] [6] [7] [8] Publication Abstract from PubMedA synaptic complex of Tn5 transposase with an extended outside end DNA duplex was prepared and crystallized, and its crystal structure was determined in an effort to reveal the role of metal ions in catalysis. Two Mn2+ ions bound to the active site when a single nucleotide of donor DNA was added to the 3' end of the transferred strand. Marked conformational changes were observed in the DNA bases closest to the active site. The position of the metal ions and the conformational changes of the DNA provide insight into the mechanism of hairpin formation and cleavage, and is consistent with a two-metal model for catalysis. Two-metal active site binding of a Tn5 transposase synaptic complex.,Lovell S, Goryshin IY, Reznikoff WR, Rayment I Nat Struct Biol. 2002 Apr;9(4):278-81. PMID:11896402[9] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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