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Arginase is a manganese-dependent metalloenzyme that catalyzes the hydrolysis of L-arginine to L-ornithine and urea. The product L-ornithine is an important component which has wide applications in the healthcare and pharmaceutical industry. Enzymatic biosynthesis of L-ornithine is one of the effective methods in which arginase is used as a bio-catalyst. Here, we report the crystal structure of arginase from  Thermus thermophilus  ( Tt Arginase) in three different crystal forms. All structures were solved by molecular replacement and refined at 2.0 Å, 2.3 Å and 2.91 Å resolution respectively.  Tt Arginase is compared with other structural homologs and the putative catalytic site residues were identified. To understand the thermophilic nature of  Tt Arginase, the sequence and structural factors of  Tt Arginase was compared with its mesophilic counterpart  Bacillus subtilis  arginase  (Bs Arginase). To get insights on structural stability, molecular dynamics (MD) simulations were carried for  Tt Arginase and  Bs Arginase at three different temperatures (300 K, 333 K and 353 K). The results indicate that  Tt Arginase is comparatively more stable than  Bs Arginase. MD simulations were carried out in the absence of the metal ions at the active site which revealed high plasticity of the active site. The results suggest that metal ions are critical not only for the catalytic function, but also required for the maintenance of the proper active site geometry. Since arginase can be employed for large-scale industrial production of L-ornithine, the structural details of thermophilic arginases such as  Tt Arginase will be helpful to engineer the protein to optimize its enzymatic action in a variety of conditions. Communicated by Ramaswamy H. Sarma

Crystal structure analysis and molecular dynamics simulations of arginase from Thermus thermophilus