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Volume 11
Journal of Proteomics & Bioinformatics
ISSN: 0974-276X
Structural Biology 2018
September 24-26, 2018
September 24-26, 2018 | Berlin, Germany
14
th
International Conference on
Structural Biology
Structure and specificity of the arginine repressor (ArgR) from
Corynebacterium pseudotuberculosis
R K Arni, R B Mariutti
and
J E Hernández
IBILCE - UNESP, Brazil
P
athogenic 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 MA, Caruso I P, Oliveira VM, 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,
CoronadoMA,NaderHB, Senff-RibeiroA, ChaimOM, Arni RKandVeiga S S (2016)Active sitemappingof 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
R K Arni is a Full Professor in Multiuser Center for Biomolecular Innovation, Department of Physics, IBILCE/UNESP, Brazil. His research interest includes: structural
molecular biology, biochemistry, biophysics, crystallography, NMR with emphasis on blood coagulation, toxins, plant viral proteins, industrial and bacterial enzymes.
R K Arni et al., J Proteomics Bioinform 2018, Volume 11
DOI: 10.4172/0974-276X-C2-116