Terminal residues modulate DNA-binding site size and stability of the SSB-like DNA-binding protein Gp13 from bacteriophage Phi11
Vivek Ratre, Malabika Biswas · 2026
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Description
Vivek Ratre and Malabika Biswas examine a DNA-binding protein in a 2026 laboratory study. The protein is Gp13 from bacteriophage Phi11, and it binds single-stranded DNA. It has an oligonucleotide and oligosaccharide-binding fold near one end and works as a pair.
The team made versions of Gp13 with small parts cut from either end. Cutting a few end residues weakened DNA binding and shrank the binding site size. Larger cuts at the front end stopped binding, which flags a key stretch of residues. Most altered proteins stayed paired, so the pairing region lies elsewhere. The work shows how the ends tune both grip and stability.
Catalog record
| CREATOR | Vivek Ratre, Malabika Biswas |
|---|---|
| YEAR | 2026 |
| COLLECTION | PAPERS |
| FORMAT | TXT |
| FILE SIZE | 41 KB |
| VERSION | 1.0 |
| LICENSE | CC BY 4.0 |
| RIGHTS | CC BY |
| SOURCE | Europe PMC |