4J7A: Crystal Structure Of Est25 - A Bacterial Homolog Of Hormone-sensitive Lipase From A Metagenomic Library

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 A resolution; it exhibits an alpha/beta-hydrolase fold consisting of a central beta-sheet enclosed by alpha-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.
PDB ID: 4J7ADownload
MMDB ID: 116622
PDB Deposition Date: 2013/2/13
Updated in MMDB: 2014/01
Experimental Method:
x-ray diffraction
Resolution: 1.49  Å
Source Organism:
Similar Structures:
Biological Unit for 4J7A: dimeric; determined by author and by software (PISA)
Molecular Components in 4J7A
Label Count Molecule
Proteins (2 molecules)
Molecule annotation
* Click molecule labels to explore molecular sequence information.

Citing MMDB