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-Structure paper
Title | Structure of a P element transposase-DNA complex reveals unusual DNA structures and GTP-DNA contacts. |
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Journal, issue, pages | Nat Struct Mol Biol, Vol. 26, Issue 11, Page 1013-1022, Year 2019 |
Publish date | Oct 28, 2019 |
Authors | George E Ghanim / Elizabeth H Kellogg / Eva Nogales / Donald C Rio / |
PubMed Abstract | P element transposase catalyzes the mobility of P element DNA transposons within the Drosophila genome. P element transposase exhibits several unique properties, including the requirement for a ...P element transposase catalyzes the mobility of P element DNA transposons within the Drosophila genome. P element transposase exhibits several unique properties, including the requirement for a guanosine triphosphate cofactor and the generation of long staggered DNA breaks during transposition. To gain insights into these features, we determined the atomic structure of the Drosophila P element transposase strand transfer complex using cryo-EM. The structure of this post-transposition nucleoprotein complex reveals that the terminal single-stranded transposon DNA adopts unusual A-form and distorted B-form helical geometries that are stabilized by extensive protein-DNA interactions. Additionally, we infer that the bound guanosine triphosphate cofactor interacts with the terminal base of the transposon DNA, apparently to position the P element DNA for catalysis. Our structure provides the first view of the P element transposase superfamily, offers new insights into P element transposition and implies a transposition pathway fundamentally distinct from other cut-and-paste DNA transposases. |
External links | Nat Struct Mol Biol / PubMed:31659330 / PubMed Central |
Methods | EM (single particle) |
Resolution | 3.6 - 4.0 Å |
Structure data | EMDB-20254, PDB-6p5a: EMDB-20321: asymmetric |
Chemicals | ChemComp-GTP: ChemComp-MG: |
Source |
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Keywords | TRANSFERASE/DNA / transposase / Strand Transfer Complex / TRANSFERASE-DNA complex / TRANSFERASE-DNA |