Crystal structure of Pelagibacterium halotolerans PE8: New insight into its substrate-binding pattern.

ABSTRACT: Lysophospholipase_carboxylesterase (LPCE) has highly conserved homologs in many diverse species ranging from bacteria to humans, as well as substantial biological significance and potential therapeutic implications. However, its biological function and catalytic mechanism remain minimally investigated because of the lack of structural information. Here, we report the crystal structure of a bacterial esterase PE8 belonging to the LPCE family. The crystal structure of PE8 was solved with a high resolution of 1.66 Å. Compared with other homologs in the family, significant differences were observed in the amino acid sequence, three-dimensional structure, and substrate-binding pattern. Residue Arg79 undergoes configuration switching when binding to the substrate and forms a unique wall, leading

SUBMITTER: Huo YY 

PROVIDER: S-EPMC5493697 | biostudies-literature | 2017 Jun

REPOSITORIES: biostudies-literature