6dgc | pdb_00006dgc

Crystal structure of the C-terminal catalytic domain of ISC1926 TnpA, an IS607-like serine recombinase

spinqualitylabelsall models 6dgc, resolution 2.92Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6dgc is a 4 chain structure with sequence from Sulfolobus sp. L00 11. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.92Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q5MPE7_9CREN Publication Abstract from PubMed IS607-family transposons are unusual because they do not have terminal inverted repeats or generate target site duplications. They encode two protein-coding genes, but only tnpA is required for transposition. Our X-ray structures confirm that TnpA is a member of the serine recombinase (SR) family, but the chemically-inactive quaternary structure of the dimer, along with the N-terminal location of the DNA binding domain, are different from other SRs. TnpA dimers from IS1535 cooperatively associate with multiple subterminal repeats, which together with additional nonspecific binding, form a nucleoprotein filament on one transposon end that efficiently captures a second unbound end to generate the paired-end complex (PEC). Formation of the PEC does not require a change in the dimeric structure of the catalytic domain, but remodeling of the C-terminal alpha-helical region is involved. We posit that the PEC recruits a chemically-active conformer of TnpA to the transposon end to initiate DNA chemistry. Multiple serine transposase dimers assemble the transposon-end synaptic complex during IS607-family transposition.,Chen W, Mandali S, Hancock SP, Kumar P, Collazo M, Cascio D, Johnson RC Elife. 2018 Oct 5;7. pii: 39611. doi: 10.7554/eLife.39611. PMID:30289389 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Transposase 3D structures

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