Hydrolytic potential of the ammonia-oxidizing Thaumarchaeon Nitrososphaera gargenis - crystal structure and activity profiles of carboxylesterases linked to their metabolic function
EstN2 is a novel alpha/beta-hydrolase originating from the ammonia-oxidizing thaumarchaeon Candidatus Nitrososphaera gargensis. The genome of the organism was sequenced and genes conferring putative lipolytic activity were amplified and cloned into Escherichia coli as a heterologous host. Through function-based screening, esterase and lipase activity was detected. A recombinant enzyme designated EstN2 was successfully expressed, purified and crystallized. The crystals belonged to space group I2, with one molecule per asymmetric unit, and diffracted X-rays to 1.5 A resolution.
        
Representative scheme of 6_AlphaBeta_hydrolase structure and an image from PDBsum server
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Databases
PDB-Sum
5A62 Previously Class, Architecture, Topology and Homologous superfamily - PDB-Sum server
FSSP
5A62Fold classification based on Structure-Structure alignment of Proteins - FSSP server