5TH3
Restriction/modification system-Type II R.SwaI cleaved DNA complex
Summary for 5TH3
Entry DOI | 10.2210/pdb5th3/pdb |
Related | 5TGQ 5TGX |
Descriptor | R-SwaI protein, DNA (cleaved 25-MER, portion 1), DNA (cleaved 25-MER, portion 2), ... (9 entities in total) |
Functional Keywords | i-swai, cleaved dna complex, r/m system, dna binding protein |
Biological source | Staphylococcus warneri More |
Total number of polymer chains | 12 |
Total formula weight | 141947.04 |
Authors | Shen, B.W.,Stoddard, B.L. (deposition date: 2016-09-29, release date: 2016-12-21, Last modification date: 2024-10-30) |
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 (2.33 Å) |
Structure validation
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