Kim_2019_PLoS.One_14_e0210298

Reference

Title : Crystal structure of chloramphenicol-metabolizing enzyme EstDL136 from a metagenome - Kim_2019_PLoS.One_14_e0210298
Author(s) : Kim SH , Kang PA , Han K , Lee SW , Rhee S
Ref : PLoS ONE , 14 :e0210298 , 2019
Abstract :

Metagenomes often convey novel biological activities and therefore have gained considerable attention for use in biotechnological applications. Recently, metagenome-derived EstDL136 was found to possess chloramphenicol (Cm)-metabolizing features. Sequence analysis showed EstDL136 to be a member of the hormone-sensitive lipase (HSL) family with an Asp-His-Ser catalytic triad and a notable substrate specificity. In this study, we determined the crystal structures of EstDL136 and in a complex with Cm. Consistent with the high sequence similarity, the structure of EstDL136 is homologous to that of the HSL family. The active site of EstDL136 is a relatively shallow pocket that could accommodate Cm as a substrate as opposed to the long acyl chain substrates typical of the HSL family. Mutational analyses further suggested that several residues in the vicinity of the active site play roles in the Cm-binding of EstDL136. These results provide structural and functional insights into a metagenome-derived EstDL136.

PubMedSearch : Kim_2019_PLoS.One_14_e0210298
PubMedID: 30645605
Gene_locus related to this paper: 9bact-g3cr02

Related information

Substrate Florfenicol    Chloramphenicol-diacetate    Chloramphenicol
Gene_locus 9bact-g3cr02
Structure 6AAE    6IEY

Citations formats

Kim SH, Kang PA, Han K, Lee SW, Rhee S (2019)
Crystal structure of chloramphenicol-metabolizing enzyme EstDL136 from a metagenome
PLoS ONE 14 :e0210298

Kim SH, Kang PA, Han K, Lee SW, Rhee S (2019)
PLoS ONE 14 :e0210298