6QH0
The complex structure of hsRosR-S5 (VNG0258H/RosR-S5)
Summary for 6QH0
| Entry DOI | 10.2210/pdb6qh0/pdb |
| Descriptor | hsRosR DNA binding protein, DNA (28-MER), SULFATE ION, ... (6 entities in total) |
| Functional Keywords | halophiles, whth dna binding protein, rosr, high salt medium, dna binding protein, protein-dna interactions |
| Biological source | Halobacterium salinarum NRC-1 More |
| Total number of polymer chains | 8 |
| Total formula weight | 89622.15 |
| Authors | Shaanan, B.,Kutnowski, N. (deposition date: 2019-01-14, release date: 2019-07-10, Last modification date: 2024-01-24) |
| Primary citation | Kutnowski, N.,Shmulevich, F.,Davidov, G.,Shahar, A.,Bar-Zvi, D.,Eichler, J.,Zarivach, R.,Shaanan, B. Specificity of protein-DNA interactions in hypersaline environment: structural studies on complexes of Halobacterium salinarum oxidative stress-dependent protein hsRosR. Nucleic Acids Res., 47:8860-8873, 2019 Cited by PubMed Abstract: Interactions between proteins and DNA are crucial for all biological systems. Many studies have shown the dependence of protein-DNA interactions on the surrounding salt concentration. How these interactions are maintained in the hypersaline environments that halophiles inhabit remains puzzling. Towards solving this enigma, we identified the DNA motif recognized by the Halobactrium salinarum ROS-dependent transcription factor (hsRosR), determined the structure of several hsRosR-DNA complexes and investigated the DNA-binding process under extreme high-salt conditions. The picture that emerges from this work contributes to our understanding of the principles underlying the interplay between electrostatic interactions and salt-mediated protein-DNA interactions in an ionic environment characterized by molar salt concentrations. PubMed: 31310308DOI: 10.1093/nar/gkz604 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.436 Å) |
Structure validation
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