TY - DATA T1 - Dataset for: NMR Elucidation of Monomer-dimer transition and Conformational heterogeneity in Histone-like DNA binding protein of Helicobacter pylori (Hup) PY - 2018/01/22 AU - Nancy Jaiswal AU - Nisha Raikwal AU - Himanshu Pandey AU - Nipanshu Agarwal AU - Ashish Arora AU - Poluri Krishna Mohan AU - Dinesh Kumar UR - https://wiley.figshare.com/articles/dataset/Dataset_for_NMR_Elucidation_of_Monomer-dimer_transition_and_Conformational_heterogeneity_in_Histone-like_DNA_binding_protein_of_i_Helicobacter_pylori_i_Hup_/5696431 DO - 10.6084/m9.figshare.5696431.v1 L4 - https://ndownloader.figshare.com/files/9979792 KW - Helicobacter pylori KW - Histone like DNA Binding Protein KW - NMR Resonance assignments KW - Secondary Structure KW - Multiple conformations KW - Conformational Heterogeneity KW - monomer dimer equilibrium KW - NMR Spectroscopy KW - Structural Biology N2 - Helicobacter pylori (H. pylori) colonizes under harsh acidic/oxidative stress conditions of human gastrointestinal tract and can survive there for infinitely longer durations of host life. The bacterium expresses several harbinger proteins to facilitate its persistent colonization under such conditions. One such protein in H. pylori is Histone like DNA binding protein (Hup) which in its homo-dimeric form binds to DNA to perform various DNA dependent cellular activities. Further, it also plays an important role in protecting the genomic DNA from oxidative stress and acidic denaturation. Legitimately, if the binding of Hup to DNA is suppressed, it will directly impact on the survival of the bacterium, thus making Hup a potential therapeutic target for developing new anti-H. pylori agents. However, to inhibit the binding of Hup to DNA, it is necessary to gain detailed insights into the molecular and structural basis of Hup-dimerization and its binding mechanism to DNA. As a first step in this direction, we report here the NMR assignments and structural features of Hup at pH of 6.0. The study revealed the occurrence of dynamic equilibrium between its monomer and dimer conformations. The dynamic equilibrium was found shifting towards dimer both at low temperature and pH; whereas DNA binding studies evidenced that the protein binds to DNA in its dimeric form. These preliminary investigations correlate very well with the diverse functionality of protein and will form the basis for future studies aiming to develop novel anti-H. pylori agents employing structure-based-rational drug discovery approach. ER -