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6QFD

The complex structure of hsRosR-S4 (vng0258/RosR-S4)

Summary for 6QFD
Entry DOI10.2210/pdb6qfd/pdb
DescriptorDNA-binding protein, DNA (28-MER), SULFATE ION, ... (6 entities in total)
Functional Keywordshalophiles, whth dna binding protein, rosr, high salt medium, dna binding protein, protein-dna interactions
Biological sourceHalobacterium salinarum NRC-1
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Total number of polymer chains8
Total formula weight90173.19
Authors
Shaanan, B.,Kutnowski, N. (deposition date: 2019-01-10, release date: 2019-07-10, Last modification date: 2024-01-24)
Primary citationKutnowski, 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: 31310308
DOI: 10.1093/nar/gkz604
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.133 Å)
Structure validation

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数据于2024-10-30公开中

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