Three-Dimensional Structure of Single-Point Mutant of Esterase PMGL2

Enzymes from extremophilic organisms are of great interest in biotechnology because they possess natural adaptation to extreme conditions often required in biotechnological processes. Lipases are a large class of hydrolytic enzymes, which catalyze the cleavage of ester bonds in triacylglycerols and have numerous biotechnological applications. The structure of a single-point mutant of esterase PMGL2 was studied. The gene encoding this enzyme was identified by the screening of a Siberian permafrost metagenomic DNA library. The structure of the mutant was determined at 1.5 Å resolution and is compared with wild-type PMGL2 in relation to the structures of the subunit, the functional dimer, and the active site of the enzyme.