Studies on Crystallization of Peptidyl-prolyl cis-trans Isomerase and AreB from Aspergillus flavus

Aspergillus flavusis a disease causative agent of many agriculture plants, common hosts are cereal grains, legumes, and tree nuts. Many strains produce a significant quantity of toxins named as mycotoxins. A. flavusis also an opportunistic pathogen of human and animals, that cause aspergillosisin immunocompromised individuals.A. flavushas Peptidyl-prolyl cis-trans isomerases (PPIase), which catalyze the isomerization of peptide bonds preceding proline residues, a process of high valuable for correct folding.PPIase belongs to the superfamily of a protein named as cyclophilin, which found in eukaryotic, bacterial and archaea.AreB hypothetical protein is similar to GATA transcription factors maintain transcription during growth and differentiation by identifying distinct GATA sites with a tandem of two conserved zinc fingers. Both zinc fingers wrap around a palindromic GATA site. This study will examine the protein structure from the X-ray crystals of PPIase and AreB and the structure determination of PPIase and AreB among the different species of A. flavus.