The lac repressor hinge helix in context: The effect of the DNA binding domain and symmetry
| Autor: | Danielle Seckfort, Gillian C. Lynch, B. Montgomery Pettitt |
|---|---|
| Rok vydání: | 2020 |
| Předmět: |
DNA
Bacterial Operator (biology) Protein Conformation Biophysics Hinge Context (language use) Molecular Dynamics Simulation Lac repressor 010402 general chemistry 01 natural sciences Biochemistry Article 03 medical and health sciences chemistry.chemical_compound Escherichia coli Lac Repressors Molecular Biology Gene 030304 developmental biology 0303 health sciences Chemistry DNA-binding domain 0104 chemical sciences Helix Thermodynamics DNA |
| Zdroj: | Biochim Biophys Acta Gen Subj |
| ISSN: | 0304-4165 |
| Popis: | The Lac system of genes has been an important model system in understanding gene regulation. When the dimer lac repressor protein binds to the correct DNA sequence, the hinge region of the protein goes through a disorder to order transition. The hinge region is disordered when binding to nonoperator sequences. This region of the protein must pay a conformational entropic penalty to order when it is bound to operator DNA. Structural studies show that this region is flexible. Previous simulations showed that this region is disordered when free in solution without the DNA binding domain present. Our simulations corroborate that this region is extremely flexible in solution, but we find that the presence of the DNA binding domain proximal to the hinge helix and salt make the ordered conformation more favorable even without DNA present. |
| Databáze: | OpenAIRE |
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