5HOO

Crystal structure of the Mos1 Strand Transfer Complex

Summary for 5HOO

• Entry DOI: 10.2210/pdb5hoo/pdb
• Related: 3HOS 3HOT 4R79 4U7B
• Descriptor: Mariner Mos1 transposase, Mos1 IR DNA NTS, Mos1 IR TS joined to Target DNA,Mos1 IR TS joined to Target DNA, ... (6 entities in total)
• Functional Keywords: protein-dna complex, dna transposase, recombinase, integrase, helix-turn-helix, base flipping, dna
• Biological source: Drosophila mauritiana (Fruit fly); More
• Cellular location: Nucleus : Q7JQ07
• Total number of polymer chains: 8
• Total formula weight: 125415.52

Authors

Richardson, J.M.,Morris, E.R. (deposition date: 2016-01-19, release date: 2016-06-01, Last modification date: 2024-11-06)

Primary citation

Morris, E.R.,Grey, H.,McKenzie, G.,Jones, A.C.,Richardson, J.M.
A bend, flip and trap mechanism for transposon integration.
Elife, 5:-, 2016

PubMed Abstract: Cut-and-paste DNA transposons of the mariner/Tc1 family are useful tools for genome engineering and are inserted specifically at TA target sites. A crystal structure of the mariner transposase Mos1 (derived from Drosophila mauritiana), in complex with transposon ends covalently joined to target DNA, portrays the transposition machinery after DNA integration. It reveals severe distortion of target DNA and flipping of the target adenines into extra-helical positions. Fluorescence experiments confirm dynamic base flipping in solution. Transposase residues W159, R186, F187 and K190 stabilise the target DNA distortions and are required for efficient transposon integration and transposition in vitro. Transposase recognises the flipped target adenines via base-specific interactions with backbone atoms, offering a molecular basis for TA target sequence selection. Our results will provide a template for re-designing mariner/Tc1 transposases with modified target specificities.

PubMed: 27223327
DOI: 10.7554/eLife.15537

Experimental method

X-RAY DIFFRACTION (3.3 Å)