Ontology highlight
ABSTRACT:
SUBMITTER: Boyko KM
PROVIDER: S-EPMC7824956 | biostudies-literature | 2021 Jan
REPOSITORIES: biostudies-literature
Boyko Konstantin M KM Kryukova Mariya V MV Petrovskaya Lada E LE Kryukova Elena A EA Nikolaeva Alena Y AY Korzhenevsky Dmitry A DA Lomakina Galina Yu GY Novototskaya-Vlasova Ksenia A KA Rivkina Elizaveta M EM Dolgikh Dmitry A DA Kirpichnikov Mikhail P MP Popov Vladimir O VO
Biomolecules 20210105 1
The gene coding for a novel cold-active esterase PMGL3 was previously obtained from a Siberian permafrost metagenomic DNA library and expressed in <i>Escherichia coli</i>. We elucidated the 3D structure of the enzyme which belongs to the hormone-sensitive lipase (HSL) family. Similar to other bacterial HSLs, PMGL3 shares a canonical α/β hydrolase fold and is presumably a dimer in solution but, in addition to the dimer, it forms a tetrameric structure in a crystal and upon prolonged incubation at ...[more]