6P5A

Drosophila P element transposase strand transfer complex

Summary for 6P5A

• Entry DOI: 10.2210/pdb6p5a/pdb
• EMDB information: 20254
• Descriptor: Transposable element P transposase, DNA (5'-D(P*CP*GP*AP*AP*CP*TP*AP*TP*A)-3'), DNA (5'-D(P*AP*GP*GP*TP*GP*GP*TP*CP*CP*CP*GP*TP*CP*GP*G)-3'), ... (7 entities in total)
• Functional Keywords: transposase, strand transfer complex, transferase-dna complex, transferase/dna
• Biological source: Drosophila melanogaster (Fruit fly); More
• Total number of polymer chains: 10
• Total formula weight: 246233.68

Authors

Kellogg, E.H.,Nogales, E.,Ghanim, G.,Rio, D.C. (deposition date: 2019-05-30, release date: 2019-10-30, Last modification date: 2024-03-20)

Primary citation

Ghanim, G.E.,Kellogg, E.H.,Nogales, E.,Rio, D.C.
Structure of a P element transposase-DNA complex reveals unusual DNA structures and GTP-DNA contacts.
Nat.Struct.Mol.Biol., 26:1013-1022, 2019

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 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.

PubMed: 31659330
DOI: 10.1038/s41594-019-0319-6

Experimental method

ELECTRON MICROSCOPY (3.6 Å)