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Structure and specificity of the arginine repressor (ArgR) from C | 44454
Journal of Proteomics & Bioinformatics

Journal of Proteomics & Bioinformatics
Open Access

ISSN: 0974-276X

Structure and specificity of the arginine repressor (ArgR) from Corynebacterium pseudotuberculosis


14th International Conference on Structural Biology

September 24-26, 2018 | Berlin, Germany

R K Arni, R B Mariutti and J E Hernandez

IBILCE - UNESP, Brazil

Posters & Accepted Abstracts: J Proteomics Bioinform

Abstract :

Pathogenic bacteria have developed a range of molecular strategies to invade and colonize host organs through highly unique and specialized mechanisms that enable them to cross barriers and overcome multiple defense systems. The knowledge of structures and interactions is primordial to understanding the enantio- and stereo- specific requirements and thus to decipher the mechanisms involved in the proliferation and pathogenic spread. This cluster of information is important to combat pathogens and in recent years, our research focus has been on bacterial inhibition through the arginine repressor (ArgR) of Corynebacterium pseudotuberculosis which plays a central role in the proliferation and spread of the pathogen in the host. The arginine repressor protein (ArgR), coordinates the expression of genes involved in arginine biosynthesis. At a certain concentration of arginine in the cytoplasm, Arg interacts with ArgR and the complex formed couples to the DNA promoter interrupting the functioning of the pathway. We have solved the structures of native and mutant ArgR and complexes at high resolution and have used molecular dynamics to characterize the specificity of the ArgR pocket and the role of the sodium ion. Recent Publications: 1. Eberle R J, Kawai L A, de Moraes F R, Tasic L, Arni R K and Coronado M A (2018) Biochemical and biophysical characterization of a mycoredoxin protein glutaredoxin A1 from Corynebacterium pseudotuberculosis. International Journal of Biological Macromolecules DOI: 10.1016/j.ijbiomac.2017.10.063. 2. Coronado M A, Caruso I P, Oliveira V M, Contessoto V G, Leite V B P, Kawai L A, Arni R K and Eberle R J (2017) Cold shock protein a from Corynebacterium pseudotuberculosis: role of electrostatic forces in the stability of the secondary structure. Protein and Peptide Letters DOI: 10.2174/0929866524666170207153808. 3. Mariutti R B, Chaves-Moreira D, Vuitika L, Caruso Í P, Coronado M A, Azevedo VA, Murakami M T, Veiga S S and Arni R K (2017) Bacterial and arachnid Sphingomyelinases D: comparison of biophysical and pathological activities. Journal of Cellular Biochemistry DOI: 10.1002/jcb.25781. 4. Vuitika L, Chaves-Moreira D, Caruso I, Lima M A, Matsubara F H, Murakami M T, Takahashi H K, Toledo M S, Coronado M A, Nader H B, Senff-Ribeiro A, Chaim O M, Arni R K and Veiga S S (2016) Active site mapping of Loxosceles phospholipases D: Biochemical and biological features. Biochim Biophys Acta DOI: 10.1016/j.bbalip.2016.05.009. 5. Eberle R J, Coronado M A, Caruso I P, Lopes D O, Miyoshi A, Azevedo V and Arni R K (2015) Chemical and thermal influence of the [4Fe-4S]2+ cluster of A/G-specific adenine glycosylase from Corynebacterium pseudotuberculosis. Biochim Biophys Acta DOI: 10.1016/j.bbagen.2014.11.014.

Biography :

  

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