4J7A

Crystal Structure of Est25 - a Bacterial Homolog of Hormone-Sensitive Lipase from a Metagenomic Library

4J7A の概要

• エントリーDOI: 10.2210/pdb4j7a/pdb
• 分子名称: Esterase (2 entities in total)
• 機能のキーワード: alpha/beta, hydrolase
• 由来する生物種: uncultured bacterium
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 158977.72

構造登録者

Ngo, T.D.,Ryu, B.H.,Ju, H.S.,Jang, E.J.,Park, K.S.,Joo, S.B.,Kim, K.K.,Kim, D.H. (登録日: 2013-02-13, 公開日: 2014-01-15, 最終更新日: 2024-03-20)

主引用文献

Ngo, T.D.,Ryu, B.H.,Ju, H.,Jang, E.,Park, K.,Kim, K.K.,Kim, D.H.
Structural and functional analyses of a bacterial homologue of hormone-sensitive lipase from a metagenomic library
Acta Crystallogr.,Sect.D, 69:1726-1737, 2014

PubMed Abstract: Intracellular mobilization of fatty acids from triacylglycerols in mammalian adipose tissues proceeds through a series of lipolytic reactions. Among the enzymes involved, hormone-sensitive lipase (HSL) is noteworthy for its central role in energy homeostasis and the pathogenic role played by its dysregulation. By virtue of its broad substrate specificity, HSL may also serve as an industrial biocatalyst. In a previous report, Est25, a bacterial homologue of HSL, was identified from a metagenomic library by functional screening. Here, the crystal structure of Est25 is reported at 1.49 Å resolution; it exhibits an α/β-hydrolase fold consisting of a central β-sheet enclosed by α-helices on both sides. The structural features of the cap domain, the substrate-binding pocket and the dimeric interface of Est25, together with biochemical and biophysical studies including native PAGE, mass spectrometry, dynamic light scattering, gel filtration and enzyme assays, could provide a basis for understanding the properties and regulation of hormone-sensitive lipase (HSL). The increased stability of cross-linked Est25 aggregates (CLEA-Est25) and their potential for extensive reuse support the application of this preparation as a biocatalyst in biotransformation processes.

PubMed: 23999296
DOI: 10.1107/S0907444913013425

実験手法

X-RAY DIFFRACTION (1.492 Å)