7BZH
Solution structure of a DNA binding protein from Sulfolobus islandicus
Summary for 7BZH
| Entry DOI | 10.2210/pdb7bzh/pdb |
| NMR Information | BMRB: 36352 |
| Descriptor | Sul7s (1 entity in total) |
| Functional Keywords | archaea, crenarchaea, sulfolobus, dna binding protein |
| Biological source | Sulfolobus islandicus |
| Total number of polymer chains | 1 |
| Total formula weight | 7226.36 |
| Authors | |
| Primary citation | Huang, C.,Liu, X.,Chen, Y.,Zhou, J.,Li, W.,Ding, N.,Huang, L.,Chen, J.,Zhang, Z. A Novel Family of Winged-Helix Single-Stranded DNA-Binding Proteins from Archaea. Int J Mol Sci, 23:-, 2022 Cited by PubMed Abstract: The winged helix superfamily comprises a large number of structurally related nucleic acid-binding proteins. While these proteins are often shown to bind dsDNA, few are known to bind ssDNA. Here, we report the identification and characterization of Sul7s, a novel winged-helix single-stranded DNA binding protein family highly conserved in . Sul7s from binds ssDNA with an affinity approximately 15-fold higher than that for dsDNA in vitro. It prefers binding oligo(dT) over oligo(dC) or a dG-rich 30-nt oligonucleotide, and barely binds oligo(dA). Further, binding by Sul7s inhibits DNA strand annealing, but shows little effect on the melting temperature of DNA duplexes. The solution structure of Sul7s determined by NMR shows a winged helix-turn-helix fold, consisting of three α-helices, three β-strands, and two short wings. It interacts with ssDNA via a large positively charged binding surface, presumably resulting in ssDNA deformation. Our results shed significant light on not only non-OB fold single-stranded DNA binding proteins in Archaea, but also the divergence of the winged-helix proteins in both function and structure during evolution. PubMed: 35408816DOI: 10.3390/ijms23073455 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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