5TGX
Restriction/modification system-Type II R-SwaI complexed with partially cleaved DNA
Summary for 5TGX
| Entry DOI | 10.2210/pdb5tgx/pdb |
| Related | 5TGQ 5TH3 |
| Descriptor | R-SwaI protein, DNA (26-MER), CALCIUM ION, ... (7 entities in total) |
| Functional Keywords | r-swai, uncleaved dna complex, r/m system, rare cutter, dna binding protein |
| Biological source | Staphylococcus warneri More |
| Total number of polymer chains | 8 |
| Total formula weight | 142327.55 |
| Authors | Shen, B.W.,Stoddard, B.L. (deposition date: 2016-09-28, release date: 2016-12-21, Last modification date: 2024-11-20) |
| Primary citation | Shen, B.W.,Heiter, D.F.,Lunnen, K.D.,Wilson, G.G.,Stoddard, B.L. DNA recognition by the SwaI restriction endonuclease involves unusual distortion of an 8 base pair A:T-rich target. Nucleic Acids Res., 45:1516-1528, 2017 Cited by PubMed Abstract: R.SwaI, a Type IIP restriction endonuclease, recognizes a palindromic eight base pair (bp) symmetric sequence, 5΄-ATTTAAAT-3΄, and cleaves that target at its center to generate blunt-ended DNA fragments. Here, we report three crystal structures of SwaI: unbound enzyme, a DNA-bound complex with calcium ions; and a DNA-bound, fully cleaved complex with magnesium ions. We compare these structures to two structurally similar ‘PD-D/ExK’ restriction endonucleases (EcoRV and HincII) that also generate blunt-ended products, and to a structurally distinct enzyme (the HNH endonuclease PacI) that also recognizes an 8-bp target site consisting solely of A:T base pairs. Binding by SwaI induces an extreme bend in the target sequence accompanied by un-pairing and re-ordering of its central A:T base pairs. This result is reminiscent of a more dramatic target deformation previously described for PacI, implying that long A:T-rich target sites might display structural or dynamic behaviors that play a significant role in endonuclease recognition and cleavage. PubMed: 28180307DOI: 10.1093/nar/gkw1200 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.3 Å) |
Structure validation
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