6dgb | pdb_00006dgb

Crystal structure of the C-terminal catalytic domain of IS1535 TnpA, an IS607-like serine recombinase

spinqualitylabelsall models 6dgb, resolution 2.52Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6dgb is a 2 chain structure with sequence from "bacillus_tuberculosis"_(zopf_1883)_klein_1884 "bacillus tuberculosis" (zopf 1883) klein 1884. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Gene: IS1535 TnpA ("Bacillus tuberculosis" (Zopf 1883) Klein 1884) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT 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.

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