8B4H
IstA transposase cleaved donor complex
Summary for 8B4H
Entry DOI | 10.2210/pdb8b4h/pdb |
EMDB information | 15848 |
Descriptor | Putative 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 Keywords | dna transposition, transposase, cleaved donor complex, dde domain, is21, ista, insertion sequence, dna binding protein |
Biological source | Geobacillus stearothermophilus More |
Total number of polymer chains | 8 |
Total formula weight | 261629.01 |
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 citation | Spinola-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: 37087515DOI: 10.1038/s41467-023-38071-x PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (3.35 Å) |
Structure validation
Download full validation report