Summary for 8Q4D
| Entry DOI | 10.2210/pdb8q4d/pdb |
| Related | 5BQ5 8B4H |
| EMDB information | 15848 18136 18144 |
| Descriptor | Putative transposase for insertion sequence element IS5376, Insertion sequence IS5376 putative ATP-binding protein, DNA (118-MER) / TIR-transferred strand, ... (8 entities in total) |
| Functional Keywords | dna transposition, dna integration, transposon, transpososome, holo-transpososome, insertion sequence, is21, ista, istb, dde transposase, dde domain, aaa+ atpase, dna strand transfer complex, stc, dna binding protein |
| Biological source | Geobacillus stearothermophilus More |
| Total number of polymer chains | 30 |
| Total formula weight | 907125.52 |
| Authors | de la Gandara, A.,Spinola-Amilibia, M.,Araujo-Bazan, L.,Nunez-Ramirez, R.,Berger, J.M.,Arias-Palomo, E. (deposition date: 2023-08-06, release date: 2024-07-10) |
| Primary citation | de la Gandara, A.,Spinola-Amilibia, M.,Araujo-Bazan, L.,Nunez-Ramirez, R.,Berger, J.M.,Arias-Palomo, E. Molecular basis for transposase activation by a dedicated AAA+ ATPase. Nature, 630:1003-1011, 2024 Cited by PubMed Abstract: Transposases drive chromosomal rearrangements and the dissemination of drug-resistance genes and toxins. Although some transposases act alone, many rely on dedicated AAA+ ATPase subunits that regulate site selectivity and catalytic function through poorly understood mechanisms. Using IS21 as a model transposase system, we show how an ATPase regulator uses nucleotide-controlled assembly and DNA deformation to enable structure-based site selectivity, transposase recruitment, and activation and integration. Solution and cryogenic electron microscopy studies show that the IstB ATPase self-assembles into an autoinhibited pentamer of dimers that tightly curves target DNA into a half-coil. Two of these decamers dimerize, which stabilizes the target nucleic acid into a kinked S-shaped configuration that engages the IstA transposase at the interface between the two IstB oligomers to form an approximately 1 MDa transpososome complex. Specific interactions stimulate regulator ATPase activity and trigger a large conformational change on the transposase that positions the catalytic site to perform DNA strand transfer. These studies help explain how AAA+ ATPase regulators-which are used by classical transposition systems such as Tn7, Mu and CRISPR-associated elements-can remodel their substrate DNA and cognate transposases to promote function. PubMed: 38926614DOI: 10.1038/s41586-024-07550-6 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (3.62 Å) |
Structure validation
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