- EMDB-18144: IstA-IstB(E167Q) Strand Transfer Complex -
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Basic information
Entry
Database: EMDB / ID: EMD-18144
Title
IstA-IstB(E167Q) Strand Transfer Complex
Map data
sharpened map
Sample
Complex: IstA-IstB(E167Q) Strand Transfer Complex
Complex: IstA-IstB(E167Q) Strand
Protein or peptide: Putative transposase for insertion sequence element IS5376
Protein or peptide: Insertion sequence IS5376 putative ATP-binding protein
Complex: DNA
DNA: DNA (118-MER) / TIR-transferred strand
DNA: DNA (58-MER) / TIR non-transferred strand
DNA: DNA (58-MER) / target-reverse complement
Ligand: MAGNESIUM ION
Ligand: ADENOSINE-5'-DIPHOSPHATE
Ligand: ADENOSINE-5'-TRIPHOSPHATE
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
Function / homology
Function and homology information
transposition / DNA strand exchange activity / DNA integration / DNA replication / ATP hydrolysis activity / DNA binding / ATP binding Similarity search - Function
HTH domain, IS21 transposase-type / IS21 transposase-type HTH domain profile. / : / DNA replication protein DnaC/insertion sequence putative ATP-binding protein / IstB-like ATP-binding protein / IstB-like ATP binding protein / Resolvase, HTH domain / Helix-turn-helix domain of resolvase / ClpA/B family / Integrase core domain ...HTH domain, IS21 transposase-type / IS21 transposase-type HTH domain profile. / : / DNA replication protein DnaC/insertion sequence putative ATP-binding protein / IstB-like ATP-binding protein / IstB-like ATP binding protein / Resolvase, HTH domain / Helix-turn-helix domain of resolvase / ClpA/B family / Integrase core domain / Integrase, catalytic core / Integrase catalytic domain profile. / Ribonuclease H superfamily / Ribonuclease H-like superfamily / ATPases associated with a variety of cellular activities / AAA+ ATPase domain / P-loop containing nucleoside triphosphate hydrolase Similarity search - Domain/homology
Putative transposase for insertion sequence element IS5376 / Insertion sequence IS5376 putative ATP-binding protein Similarity search - Component
Biological species
Geobacillus stearothermophilus (bacteria)
Method
single particle reconstruction / cryo EM / Resolution: 3.62 Å
Spanish Ministry of Science, Innovation, and Universities
PID2020-120275GB-I00
Spain
Spanish Ministry of Science, Innovation, and Universities
PRE2018-086026
Spain
Citation
Journal: Nature / Year: 2024 Title: Molecular basis for transposase activation by a dedicated AAA+ ATPase. Authors: Álvaro de la Gándara / Mercedes Spínola-Amilibia / Lidia Araújo-Bazán / Rafael Núñez-Ramírez / James M Berger / Ernesto Arias-Palomo / 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 ...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.
UniProtKB: Insertion sequence IS5376 putative ATP-binding protein
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Macromolecule #3: DNA (118-MER) / TIR-transferred strand
Macromolecule
Name: DNA (118-MER) / TIR-transferred strand / type: dna / ID: 3 Details: complete sequence of the right terminal inverted repeat (TIR) covalently bound to a target DNA Number of copies: 2 / Classification: DNA
Macromolecule #4: DNA (58-MER) / TIR non-transferred strand
Macromolecule
Name: DNA (58-MER) / TIR non-transferred strand / type: dna / ID: 4 Details: complementary sequence of the right terminal inverted repeat (TIR) Number of copies: 2 / Classification: DNA
Macromolecule #5: DNA (58-MER) / target-reverse complement
Macromolecule
Name: DNA (58-MER) / target-reverse complement / type: dna / ID: 5 / Details: complementary sequence of the target DNA / Number of copies: 2 / Classification: DNA
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