1mus

crystal structure of Tn5 transposase complexed with resolved outside end DNA

spinqualitylabelsall models 1mus, resolution 1.90Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1mus is a 3 chain structure with sequence from Escherichia coli. The December 2006 RCSB PDB Molecule of the Month feature on Transposase by David S. Goodsell is 10.2210/rcsb_pdb/mom_2006_12. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.9Å Ligands: EDO, MG, MN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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). Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. See Also Transposase 3D structures

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