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8B4H

IstA transposase cleaved donor complex

Summary for 8B4H
Entry DOI10.2210/pdb8b4h/pdb
EMDB information15848
DescriptorPutative transposase for insertion sequence element IS5376, DNA (57-MER) / right IS21 transposon end (insertion sequence IS5376), DNA (55-MER) / right IS21 transposon end (insertion sequence IS5376), ... (4 entities in total)
Functional Keywordsdna transposition, transposase, cleaved donor complex, dde domain, is21, ista, insertion sequence, dna binding protein
Biological sourceGeobacillus stearothermophilus
More
Total number of polymer chains8
Total formula weight261629.01
Authors
Spinola-Amilibia, M.,de la Gandara, A.,Araujo-Bazan, L.,Berger, J.M.,Arias-Palomo, E. (deposition date: 2022-09-20, release date: 2023-05-03, Last modification date: 2024-07-24)
Primary citationSpinola-Amilibia, M.,Araujo-Bazan, L.,de la Gandara, A.,Berger, J.M.,Arias-Palomo, E.
IS21 family transposase cleaved donor complex traps two right-handed superhelical crossings.
Nat Commun, 14:2335-2335, 2023
Cited by
PubMed Abstract: Transposases are ubiquitous enzymes that catalyze DNA rearrangement events with broad impacts on gene expression, genome evolution, and the spread of drug-resistance in bacteria. Here, we use biochemical and structural approaches to define the molecular determinants by which IstA, a transposase present in the widespread IS21 family of mobile elements, catalyzes efficient DNA transposition. Solution studies show that IstA engages the transposon terminal sequences to form a high-molecular weight complex and promote DNA integration. A 3.4 Å resolution structure of the transposase bound to transposon ends corroborates our biochemical findings and reveals that IstA self-assembles into a highly intertwined tetramer that synapses two supercoiled terminal inverted repeats. The three-dimensional organization of the IstA•DNA cleaved donor complex reveals remarkable similarities with retroviral integrases and classic transposase systems, such as Tn7 and bacteriophage Mu, and provides insights into IS21 transposition.
PubMed: 37087515
DOI: 10.1038/s41467-023-38071-x
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.35 Å)
Structure validation

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數據於2024-11-06公開中

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