Structure of the gene 2.5 protein, a single-stranded DNA binding protein encoded by bacteriophage T7
| Autor: | James M. Stattel, Charles C. Richardson, Thomas Hollis, Tom Ellenberger, Dane S. Walther |
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| Rok vydání: | 2001 |
| Předmět: |
Models
Molecular HMG-box Protein Conformation DNA polymerase II Molecular Sequence Data DNA Single-Stranded Crystallography X-Ray Single-stranded binding protein Viral Proteins Bacteriophage T7 Amino Acid Sequence Replication protein A Binding Sites Multidisciplinary DNA clamp Sequence Homology Amino Acid biology DNA replication T7 DNA polymerase Biological Sciences Molecular biology DNA-Binding Proteins biology.protein Biophysics Primase Sequence Alignment |
| Zdroj: | Proceedings of the National Academy of Sciences. 98:9557-9562 |
| ISSN: | 1091-6490 0027-8424 |
| DOI: | 10.1073/pnas.171317698 |
| Popis: | The gene 2.5 protein (gp2.5) of bacteriophage T7 is a single-stranded DNA (ssDNA) binding protein that has essential roles in DNA replication and recombination. In addition to binding DNA, gp2.5 physically interacts with T7 DNA polymerase and T7 primase-helicase during replication to coordinate events at the replication fork. We have determined a 1.9-Å crystal structure of gp2.5 and show that it has a conserved OB-fold (oligosaccharide/oligonucleotide binding fold) that is well adapted for interactions with ssDNA. Superposition of the OB-folds of gp2.5 and other ssDNA binding proteins reveals a conserved patch of aromatic residues that stack against the bases of ssDNA in the other crystal structures, suggesting that gp2.5 binds to ssDNA in a similar manner. An acidic C-terminal extension of the gp2.5 protein, which is required for dimer formation and for interactions with the T7 DNA polymerase and the primase-helicase, appears to be flexible and may act as a switch that modulates the DNA binding affinity of gp2.5. |
| Databáze: | OpenAIRE |
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